Automatically generated rough PDF by ProofCheck from River Valley Technologies Ltd iue1: Figure forboth greatopportunities offer very However, property applications. is [10]. catalytic biotechnological DyPs and detoxification and about enzymology, knowledge chlorite peroxidase specificity our exploring anal- in substrate proteins, involved structurally heme unique other are are their to However, They that contrast proteins. limited. enzymes In unclear. heme of is of relationship group class evolutional a novel their dismutases, a as chlorite peroxidase-catalase, recognized to include been ogous families have (super) DyPs 1). recently, resulting (Figure with very haloperoxidase The enzymes Only and se- peroxidase of 9]. di-heme primary on groups [8, dismutase, based several peroxidase-chlorite cyclooxygenase, properties revealed peroxidase catalytic analysis superfamilies phylogenic and peroxidase Later, structural His- andanimal origins. cycle. distinct catalytic isolation the plant and in into alignment heme classified use quence all are they enzymes although diverse these functionally torically, and modification. structurally translational they are post but involve enzymes not degradation, These does lignin expression in functional oxidases their EC fungal as the (DyPs, manipulate to peroxidases to equivalent dye-decolorizing easier lignin- are much of enzymes contain are These class that 7]. unique [6, bacteria bacteria, a These PF04261) ligninolytic have 5]. 1.11.1.19, [4, identifying proteobacteria, degraders lignin and in be actinobacteria to interest characterized including growing been have infungi. bacteria a several fungal far, geneticmanipulation is So by and enzymes. there depolymerization degrading however, proteinexpression industrial in years, objective, recent todifficulties important due In an largely difficult, is be valorization would enzymes lignin Although which chemicals, [3]. phenolic enzymes useful into converted be it fuels. may can fossil long as units As from phenylpropane 2]. derived [1, the currently biorefineries chemicals burnt are depolymerized, for aromatic is be renewable critical provide lignin can is to example, it candidate lignin obvious For as of the applications. Valorization is low-value production. Lignin revenue. in ethanol high used generate cellulosic been in only or energy heterogene- has fuels recover inherent its to it to to converted Therefore due be processing recalcitrance. can further and for which target ity xylose), challenging a and presents Thelatter glucose lignin contrast, (e.g. andhemicellulose. In monosaccharides chemicals. give lignin fromcellulose to depolymerized with separating are two begins biomass processing biorefineries, In Introduction 1 opportunities biotechnological and properties Biochemical peroxidases: dye-decolorizing Bacterial Li Tao / Chen Chao GRUYTER DE hscneti free. is content This Berlin/Boston. Gruyter de Walter by 2016 © Chen Chao DOI: eeprxdsspa seta oe nbooia ciiis hyaeuiutu naldmiso life. of domains all in ubiquitous are They activities. biological in roles essential play peroxidases Heme oxidative and copper-containing heme- that secrete fungi by rot depolymerized efficiently is lignin nature, In 10.1515/psr-2016-0051 stecrepnigauthor. corresponding the is lsiiaino eeprxds n y-yeperoxidase. and Dyp-type peroxidase heme of Classification hsclSine eiw.21;20160051 2016; Reviews. Sciences Physical 1 Automatically generated rough PDF by ProofCheck from River Valley Technologies Ltd eoiae,bceilDP a looiieaode,AT n ml hnlccmonsicuigcate- [18]. products including sulfide sulfoxide plant catalyze compounds chiral from to to phenolic known TfuDyP small Similar are A-type an- peroxidases and peroxidases. an Similarly, synthetic Plant ABTS other oxygenation. 2,6-dimethoxyphenol. are dyes, and for ones (HQ) azo substrates hydroquinone notable oxidize poor guaiacol, most also chol, are The can which substrates. DyPs series, of bacterial range Blue peroxidases, Reactive wide a as of such oxidation thraquinones the catalyze DyPs Bacterial properties Biochemical 2 ascyan are colored proteins unclassified and purple, 2015). as 15, colored September are on proteins performed Eukaryota yellow, (Search and green as colored are 2: Figure bacterial of catalytic use underlying potential their project alternatives. to to efficient relation reviewed more in are func- as of peroxidases highlighted DyPs context of are the applications DyPs in biotechnological discussed the The are of machinery. DyPs discussed characters the are structural of features roles The kinetic physiological diversity. and The tional properties mechanism. spectral peroxidase Their of properties characterized. basis un- biochemical been the to diverse have on critical the that is review DyPs we it 38 chapter, bacterial potential, this the industrial the In of their to biocatalysis. realize to compared available, To relevant is characterized. species properties information well Bacteria their sequence are derstand DyP peroxidases 515 of the the amount of increasing handful in that a present fact only the widely Despite are 2). (Figure which species proteins, Eukaryota 14 can 7, Dyp-type they [6, putative as chemicals 889 Class biocatalysts lignin-derived in 16 and attractive dyes those be synthetic while to as bacteria, shown such from have substrates predominantly of DyPs are range bacterial C wide Many and a fromA Basidiomycota. oxidize B, classes A, from four Classes largely into in are classified peroxidases further D The are 1). DyPs (Figure the anthraquinone Therefore, (3.0 D of low. oxidation optimum to is the pH catalyze identity all low sequence they primary with Although prokaryotes. dyes their in dyes, anthraquinone found later on been activity have novel DyPs More has 13]. It peroxidases. known other all 2 candidum atra ysaearc oreo ictlss o ntne eetsac ftePa aaaerevealed database Pfam the of search recent a instance, For biocatalysts. of source rich a are DyPs Bacterial h is y-yepoenwsioae n1999from in wasisolated protein Dyp-type first The hnadLi and Chen itiuino y-yeprxdssars pce.I saatdfo h fmdtbs 1] atraproteins Bacteria [17]. database Pfam the from adapted is It species. across peroxidases Dyp-type of Distribution e ,DyP 1, Dec Dec ) y-eooiigfnu 1] h nyei lcpoenwt o oooyto homology low with glycoprotein a is enzyme The [11]. fungus dye-decolorizing a 1), hroiiafusca Thermobifida hntpou cucumeris Thanatephorus a eotdt ovr rmtcslieto sulfide aromatic convert to reported was e (formerly 1 Dec – 16]. Geotrichum EGRUYTER DE – .)[12, 3.2) Automatically generated rough PDF by ProofCheck from River Valley Technologies Ltd o rntasotto n pae[5.Fna ysas aesonoyeaeo yrls ciiis[36], heme activities from hydrolase iron or oxygenase of shown removal have the also deferrochelation, DyPs catalyze Fungal to [35]. uptake proposed and was transportation Mn DyP iron by A-type for mediated An is 34]. reaction [7, This required anisaldehyde. to MMA from the as DyPs bacterial by degradation lignin facilitate can mediator. manganese redox that support strongly examples from These Mn 33]. DyP2 of addition C-type the upon by the lignocelluloses magnitude straw is in 10 of wheat DyP active degrade orders manganese-reactive manganese to three most found be by was the to turnover shortened DyP1B found enzymes, is the were the half-life in paralogs of the increase One DyP which 80-fold B-type of Two an I, [31]. in compound mutation resulted of Ala reactivity higher with the DypB the modifying Mn of by of Asn246 oxidation is improvable of of thisefficiency substitution 30]. However, [29, The MnCl DyP. mM peroxidases bacterial manganese 1 fide of bona presence of the that than in only active is of Mn DypB efficiency digestion, enzymes. lignocellulose these by straw have degradation wheat lignin activities for In manganese critical from far, be can DypB So activity This example, DyPs. 1). (Table For bacterial DyPs C-type with and lignin B- in of found been degradation oxidative for mediator desirable H equivalent one cycle, catalytic the In Mn oxidizes 3: Figure substrates potential redox low for those while °C, °C. 50 30 its at BsDyP, at reached in appeared that compounds example, For shown model have cases. lignin some also on in activities studies dependent maximal biochemical substrate Notably, is 16]. activity demonstrated peroxidative [6, been for mediators have optimum redox DyPs temperature B-type without and lignin A- Moreover, Kraft [13]. decompose product to BsDyPfrom the as DyP [15]. anisaldehyde give to MMA byabacterial oxidize ( syringaldehyde against activities dimer peroxidase nonphenolic displayed ofdecomposing example first the from BsDyP activities. ing Two 25]. 18, [15, ( alcohol veratryl including DyPs compounds bacterial glycerol- some Remarkably, model 14]. lignin [6, nonphenolic conditions on reaction active and are DyP the on depending polymerization, or tion of degradation The [24]. sp Amycolatopsis from TcDyP potential. redox high quires GRUYTER DE iia usrt ag,fna ysaegnrlymr fiin hntoefo atrai h xdto of the oxidation in 23]. [14, activity bacteria comparable from have DyPs those bacterial than few efficient a Only more RB5. generally classes have and are fromdifferent ABTS DyPs DyPs fungal Although 1). range, substrate (Table peroxidases similar different compare to parameters common the cooperation of suggesting Michaelis [14], the constant on dyes based Michaelis curves saturation apparent [19 and anthraquinone to peroxidases data ABTS versatile kinetic and ting of DyPs fungal like the oxidation sites oxidation in multiple profiles TcDyP from kinetic Forexample, [19]. sigmodial models different entail therefore mechanisms, 5 nadto,svrlbceilDP a aayeafwetariayratos y2ctlzdteconversion the catalyzed DyP2 reactions. extraordinary few a catalyze can DyPs bacterial several addition, In that enzyme fungal a is It degradation. lignin in role important an plays peroxidase manganese nature, In aybceilDP fromA DyPs bacterial Many differentkinetic have reactions many since bedifficult can of peroxidases efficiency catalytic Comparing M – 1 s tutrso innmdlcompounds. model lignin of Structures β – gaao te ( ether -guaiacol 1 Tbe1,apocigteatvt ffna agns eoiae n estl eoiae [32, peroxidases versatile and peroxidases manganese fungal of activity the approaching 1), (Table 2+ oMn to 2+ 5v 7 a xdz uiclglycerol- guaiacyl oxidize can [7] 75iv2 . ailssubtilis Bacillus xdto yteDp sol 51M 25.1 only is DypB the by oxidation 2+ (퐾 3+ 푚 oMn to 푎푝푝 hc a ifs nblylgi usrtst eops h eactatcompounds. therecalcitrant to decompose substrates lignin in bulky diffuse can which , ) 1a n h paettroe number turnover apparent the and .jostii R. 1b ailssubtilis Bacillus trswt C with starts 3+ , s26i h itlhm eiu fDp.Ti mrvmn slkl u to due likely is improvement This DypB. of residue heme distal the is Asn246 . Δ -yeDP hrn 6 rmr euneiett aeas hwdpromis- showed also have identity sequence primary 96% sharing DyPs A-type – .Vv H) n -ehxmnei cd( acid 4-methoxymandelic and NHE), vs 1.0V > E lse a eit h ietoiaino innmdlcmonsta re- that compounds model lignin of oxidation direct the mediate can classes C H1i ciae yMn by activated is RHA1 2 O .curvata T. 2 α CC03a on octlz h laaea C at cleavage the catalyze to found KCTC2023was -C xdzstoeuvlnso Mn of equivalents two oxidizes β odcevg,bttepout a eutfo ihrdegrada- either from result can products the but cleavage, bond 1] yBfrom DypB [14], – 1 β 4a s gaao te Fgr 3, (Figure ether -guaiacol – 1 n ctsrnoe( acetosyringone and ) 2] prxmtl orodr fmgiuelower magnitude of orders four approximately [28], 2+ .sp A. (퐾 2+ y5 by 푐푎푡 푎푝푝 n n diinleuvln foye is oxygen of equivalent additional one and , 5v 7,whose [7], 75iv2 . hdccu jostii Rhodococcus ) – – r sdt eemn nyeselectivity, enzyme determine to used are 3flstwr innmdlsubstrates. model lignin toward folds 23 etneuto.Tersligapparent resulting The equation. Menten – 2.Sc iuto ssmlfe yfit- by simplified is situation a Such 22]. 2+ 2] lal,mnaeei highly a is manganese Clearly, [27]. hrooopr curvata Thermomonospora 3 , 2 4b suooa fluorescens Pseudomonas Δ MMA, , 1a .Vv H) guaiacyl NHE), vs 1.4V = E 2] cy a on to found was TcDyP [26]. ) H1[]adDP from DyP2 and [6] RHA1 , 퐾 Δ 푐푎푡 푎푝푝 0.6 = E /퐾 Δ ailssubtilis Bacillus . sNHE) vs V 1.4 > E α 2 푚 푎푝푝 -C 6.Tecatalytic The [6]. – hnadLi and Chen β . sNHE) vs V 0.8 au s12× 1.2 is value of 1b 2+ hsis This . exhibits ofar, So . Pf-5. 168 3 Automatically generated rough PDF by ProofCheck from River Valley Technologies Ltd h aayi rcs yial eurstosnl-lcrnoiain ntefrtse,arsigfri enzyme ferric aresting 36]. [13, step, peroxidases first classical the of In oxidation. that single-electron to two similar requires mechanism typically the process employ catalytic to The proposed been have DyPs Bacterial DyPs bacterial of mechanism Catalytic 4 naturalsub- of roles. physiological their Theidentification unveil to critical processes. be inbiological will diverse enzymes highly these in roles for organized are different strates are DyPs many genes C-type suggesting their that However, suggest peroxidases. contexts, properties lignin-degrading genomic biochemical as The function [7]. to peroxidases likely plant more of those to clarified. activity be peroxidase to remains DypB of role the Therefore, ferritin. as such enc with For co-expressed [46]. degradation probably lignin and with co-localized associated be not may DypB of example, role physiological the that suggested evidence of deletion Also, compounds. activity a its as on YfeX based oxidase of porphyrinogen function [44]. a The III be coproporphyrinogen to [43]. and proposed activity IX been protoporphyrinogen deferrochelation has on the It controversial. in suggest- also involved fromhemin, is be deferrochlatase iron removal mechanismsmight other notcatalyze that does ing EfeB purified However, respectively. genomic overex- component, the by their uptake supported as is notion heme, This from [35]. as (PPIX) acquisition IX context, protoporphyrin iron of bacterial accumulation 99.9% the for in by resulted dechelatases pression reduced are was function mutant DyP) knockout YfeX(B-type paralog its for rate reac- H by survival mM of upregulated the 25 was and of protein strain, This addition native stress. upon the oxidative in for various species machinery from fulfill oxygen regulatory to (VNG0798H) tive proposed in DyP involved been A-type have be putative DyPs to bacterial a suggested context, example, genomic For their roles. as well physiological as reactivity their on Based DyPs bacterial of roles Physiological 3 peroxidases. versatile catalytically of group a bacterial together, be Taken to DyPs. shown bacterial been characterized have hitherto DyPs in found been not have activities these however, 4 rule isnotgeneral this Still, classes. [18, 45]. in other for substrates DyPs as TAT peptides confirmed signal the experimentally (TAT) from been have translocation DyPs roles A-type twinarginine some different only N-terminal fulfill as may unique they their So to translocation. due proteins periplasmic efeUOB C-type DyPs are more efficient catalysts than those in A- and B-type. They displayed comparable manganese displayed They B-type. A- and in those than catalysts efficient more are DyPs C-type h oaino nezm lopoie le oispyilgclrl.Atp ysaepeitdas predicted from are DyP B-type DyPs the A-type DypB, role. physiological its to clues provides also enzyme an of location The noe nasln atra cshda aooprmn,wihcnecpuaefntoa proteins functional encapsulate can which nanocompartment, icosahedral bacterial a encapsulin, encodes hnadLi and Chen .jostii R. ( ycdNOB efeB sdwsra after downstream is H1cno rwo inna oecro ore h gene The source. carbon sole as lignin on grow cannot RHA1 prni nacdi cdcsrs 4] ae td ugse htEe Yd)adits and (YcdB) EfeB that suggested study Later [42]. stress acidic in enhanced is operon ) 2 O 2 dypB 4] td on study A [41]. .jostii R. eein gene efeU H1 a ensont xdz oyei innadlgi model lignin and lignin polymeric oxidize to shown been has RHA1, and .jostii R. enc efeO .coli E. nmn atraincluding bacteria many in hc noeahg-fiiyio rnpre n aniron and transporter iron high-affinity a encode which , H1rdcdlgi erdto ciiy[] tl,other Still, [6]. activity degradation lignin reduced RHA1 eeepeso rfl hwdta the transcription that showed profile expression gene aoatru salinarum Halobacterium .jostii R. dypB ooosaefudt be to found are homologs H1[47 RHA1 – 9.Tegene The 49]. EGRUYTER DE a been has Automatically generated rough PDF by ProofCheck from River Valley Technologies Ltd n h infcneo mn cd nteactivesites. in the transformation, and acids formation of amino their of significance rate the the cycle, catalytic and measuring inperoxidase intermediates, themechanism reaction shift the the tostudy characterizing causes opportunities usually including porphyrin important offers of microenvironment change This of change bands. The these 5. of ( Figure Q in band, shown Soret as have bands DyPs (CT) of transfer spectra adsorption electronic the peroxidases, containing heme al 1: Table 5: Figure reduction. its and formation II compound formation, I compound 4: Figure 4). (Figure respectively reduction, II compound and formation I compound for ofK constants value reaction steady the represent the Although For example, equivalent [50]. Michaelis one 4) the interpretations. fit by (Figure different still kinetics peroxidase reduction typical ping-pong second a peroxidase for a data as state referred undergoes is II mechanism compound [Fe this [Fe form last, irreversible, to the and substrate restore II; reducing to compound a electron as from electron designated equivalent is one that by reduced then is [Fe high-valent species a yield to peroxide hydrogen with reacts GRUYTER DE wt-DypA Name MnP LiP HRP DyP TcDyP wt-DypB h rniino the of transition The Dec1 bopinmxm frsigsaeadoiie nemdae fhm eoiae aotdfo [14]). from (adopted peroxidases heme of intermediates oxidized and state resting of maxima Absorption pcrlcaatrsiso tTDP lutaigSrt n hre rnfr(T bands. (CT) transfer charger and Q Soret, wt-TcDyP, illustrating of characteristics Spectral k TcDyP. in mechanism kinetic ping-pong peroxidase proposed The 7.8 3.0 7.5 3.2 7.5 value pH 4.5 6.0 6.6 π 3+ eetosi eoiaeprhrngnrtsuiu VVssetu.Lk other Like spectrum. UV-Vis unique generates porphyrin peroxidase in -electrons etn tt fteprxds.Sneteeprxdtv ecin r generally are reactions peroxidative these Since peroxidase. the of state resting ] 567( 544( 508, 406, 630 573, 542( 509, 406, 634 503, 404, 0,52 632 502, 406, 630 496, 408, 640 498, 403, 636 506, 406, 632 502, 408, state Resting sh ,624 ), sh sh ), ), m – etneuto,tersligprmtr aeentirely have parameters resulting the equation, Menten o usrt stpclyk typically is substrate for 4+ 622( ( 648 623, 546, 512, 407, 646( 621, 569, ND 547, 510, 406, 648 613, 580, 400, 0,58 1,6040 2,555 528, 420, 556 525, 420, 650 617, 558, 407, 650 608, 550, 408, 525( 400, 644( 615, 556, 530, 401, ND I Compound =O] sh + ,651 ), • hti eintda opudI h oxoferryl the I; compound as designated is that sh sh sh ,577, ), ) ) sh 1 ) k , 2 n k and , 2,57 555 527, 420, ( 662 621, 549, 515, 410, 1,644( 615, 555, 529, 399, 666 623, 555, 530, 416, 1,58 5,69[28] Ref. 619 557, 528, 419, II Compound 3 ersn aecntnsfor constants rate represent 1 [H sh sh ) 2 ) O 2 ]/k 4+ α =O] 3 and hr k where , [57] [28] [13] [14] [59] [58] hnadLi and Chen + β intermediate n charge and ) 1 n k and 5 3 Automatically generated rough PDF by ProofCheck from River Valley Technologies Ltd r hw nbu,genadrdcre,rsetvl.Arw niaecagso bobneoe ie hsresearch This [51]. time. over Chemistry absorbance Biological of of changes Journal indicate the Arrows respectively. in curves, sequen- published red a originally and was in hydroquinone green with blue, H TcDyP-II in of with TcDyP-H281A shown Reaction of are C: Reaction mode. D: mixing mode. sequential mixing a tial in hydroquinone with TcDyP-I of tion 6: Figure 6 M M 600 100 ± ± 12800 2000 = = m m /Kapp /Kapp I (kapp (kapp in compound 4 ABTS peroxidases prefers that Blue two Reactive suggesting prefers are H min, DypA equivalent DypB 20 A-type more and after The one DypA state Adding resting [13]. to I. reduced compound returned is enzyme of the formation However, the changes. suggesting additional however, min, reality, H 0.2 In of in equivalent 1). band one (Table UV-Vis with only with reacting far, Upon intermediates So cucumeris complicated. reactive T. electron. more for unpaired much studied an is has been mechanism II have it the compound since DyPs and of (EPR) bacterial I addition resonance Compound few The state. paramagnetic reductant. a resting electron one-electron the by of to distinguished equivalent back be one II can adding compound convert by can out reductant carried equivalent is second I compound from II pound lws tpi Qoiain ntefl aayi yl fTDP opudI euto sterate-limiting the is reduction II compound TcDyP, the of be to cycle at out catalytic turned measured full TcDyP-0 was regenerate the to reduction TcDyP-II step. In TcDyP-II of HQ-oxidation. for reduction in that The formation TcDyP-II step while 7). for slowest (Figure pH7.8), rate band) 55]. band, The Soret [13, (TcDyP-0 Soret state. reduce (TcDyP-II nm peroxidases resting to nm 406 to and (HQ) 416 back hydroquinone DyPs TcDyP-II equivalent at converted other one HQ determined in using of was by equivalent reported achieved second been was A TcDyP has horseradish I. of TcDyP that of II compound phenomenon that spontaneously of a than intermediates formation transient state, faster The the resting fold Intriguingly, 54]. the 30 [53, to about peroxidases heme returned is many formation in TcDyP-I observed [28], been determined has DypB was 10 of constant × rate that order (1.7 to second peroxidase a similar the be is decrease change, to a this trend is using proposed this 10 By there is TcDyP-I, × nm. of other 5.92 406 formation be at the to the absorption and In band (TcDyP-I), (a)). Soret compoundI 6 the is (Figure of like) one H (TcDyP-II intermediates: product with TcDyP II-likedecay two compound of of reaction formation the the for vealed measured was transition spectral The [28]. species radical 10 ~1.80× constant rate (second-order slowly DypB while M 0.1 nter,adn H adding theory, In The cy,teAtp eoiaefrom peroxidase A-type TcDyP, the − hnadLi and Chen s − sh pcrlcagsi tTDPadTDPH8Actltccce :Rato fw-cy ihH with wt-TcDyP of Reaction A: cycle. catalytic TcDyP-H281A and wt-TcDyP in changes Spectral ) hnratn ihH with reacting When 1). n Dma hudrpa n o eetbe respectively. detectable, not and peak shoulder a mean ND and e newn nest hneo oe ekadeegneo e ek nQbnsadCT and bands Q in peaks new of emergence and peak Soret of change intensity underwent 1 Dec 6 M – 1 6 s – M 1 2 tp ..A H30 hsrt a agnlyrdcdt .6×10 × 4.06 to reduced marginally was rate this 3.0, pH At 7.8. pH at – O 1 2 s – orsigsaeDPcue h omto fcmon .Tefraino com- of formation The I. compound of formation the causes DyP state resting to 1 5] opudI-iedcypouto cy ol eapoenrdclthat radical protein a be could TcDyP of product decay II-like Compound [52]. ) 2 O 2 yAwscnetdit nitreit ihfaue fcmon II, compound of features with intermediate an into converted was DypA , .curvata T. − s 1 smr ytmtclysuidwt VVssetocp [14]. spectroscopy UV-Vis with studied systematically more is − 2 O )adas xdzsMn oxidizes also and 1) 2 cy-,TDPI n cy-I(cy-Ilk)compounds like) (TcDyP-II TcDyP-II and TcDyP-I, TcDyP-0, . 5 M .jostii R. – 1 s – 1 undit opudIlk protein-based I-like compound a into turned ) H1wt ifrn usrt specificities: substrate different with RHA1 2 O 2+ 2 − itn utwvlnt aare- data multiwavelength Fitting . s 1 kp Kp a a 51± 25.1 cat cat 1 = m /Kapp (kapp − ) hl h -yeDp cat DypB B-type the while 1), 2 O 2 h -yeDPfrom DyP D-type the , 6 M 2 O – 2 1 2 i o cause not did s O – 2 1 :Reac- B: . Although . EGRUYTER DE Automatically generated rough PDF by ProofCheck from River Valley Technologies Ltd al 2: Table experiments the inter- between the discrepancy at the interaction to strong a due no inconclusive is with is dimer DyP2 DyP2 a [7]. [18]. of as organization activity existed physiological DyP enzyme The this the face. crystallization, involve In not solution. may in dimerization oligomer that suggesting from monomer, DyP C-type a from of TfuDyP as dimer organization. active dimeric The the is 2). to DyP, exceptions (Table are observed there Nevertheless, been in- [58]. hydrophobic interaction also by has caused usually oligomerization from is order BtDyP dimerization Higher the prevent DyPs, monomers. to bacterial postulated between In are teraction which [60]. sequences, dimerization insertion analy- from C-terminal Sequence enzymes monomers. numerous exclusively the have are DyPs DyPs fungal fungal that while indicates dimers, sis in assembled mainly are DyPs Bacterial DyPs bacterial in relationship Structure-function 5 mitigated be can [56]. issue oxidation This ABTS ABTS. to as due such change substrate absorption dye eliminate a to of reaction spectrum additional the incorporating with by overlaps band Soret the when 7: Figure GRUYTER DE EfeB Proteins TyrA DypB SCO2276 SCO3963 DyP ti oeotyt eto htU-i pcrsoyhsislmtto osuyprxds mechanism peroxidase study to limitation its has spectroscopy UV-Vis that mention to noteworthy is It ito l vial tutrso atra DyPs bacterial of structures available all of List aayi yl fw-cy.Scn-re aecntnsaesoni ahse [51]. step each in shown are constants rate wt-TcDyP. Second-order of cycle Catalytic atrie htitoirnVPI-5482 thetaiotaomicron Bacteroides Amycolatopsis oneidensis Shewanella RHA1 jostii Rhodococcus coelicolor Streptomyces coelicolor Streptomyces cellulosilytica Thermobifida shrci coli Escherichia Organisms yai ih cteigmaueetsgetdta h nyeeitdas existed enzyme the that suggested measurement scattering light Dynamic . B B A A A A Class ute soitst omahxmr anyvahydrophobic via mainly hexamer, a form to associates further IZ(heme); 2IIZ Mn) (heme, 4HOV Q0SE24 N246A: DypB 3QNS(heme); 4GRC(heme) (heme) 4GT2 (heme) 4GS1 O2(heme) 3O72 2Y4F(heme); code PDB Q8EIU4 Q9RKQ2 Q9ZBW9 U3KRF5 Q8XAS4 ID Uniprot .fusca T. Dimer Hexamer Dimer Dimer Dimer Dimer structures Quaternary hnadLi and Chen nA-type an , 7 Automatically generated rough PDF by ProofCheck from River Valley Technologies Ltd nTDPas asdtels fatvt,btdtie td eelddfeetmcaim ae on transient Based mechanism. different revealed study detailed mutation but Similar activity, [18]. of disappeared loss band the Soret caused distinctive his- the also TcDyP of and substitution in binding, due the heme proposition: activity abolished this peroxidase in several alanine supported the with TfuDyP I formation reduce tidine in to analysis in compound mutagenesis expected Site-directed and involved is loss. effect histidine acid ligand pull proximal to aspartic and the between push reminiscent replacing interaction the very Therefore, The to is [64]. critical [63]. It peroxidases be Glu). metalloenzymes to or in proved (Asp been triad residue has Fe-His-Asp acidic histidine of an motif of carboxylate widespread the a to of distance bonding hydrogen in is and N the to coordinated model. cartoon including a species, elements in oxygen Structural shown and (e), are (green). residues (d), respectively. (salmon) conversed model 4G2C), stick loops surrounding code a its (PDB in heme, DyP2 shown including C-type are sites and active which respective 3QNS) code their (PDB represent DypB (f) B-type and 3O72), code (PDB EfeB type 8: Figure in residues [62]. critical 8) However, (Figure 2.5Å). relatively conserved > share highly deviation they are square C-terminal pocket) mean that the binding root revealed to (heme 32, types binding < B different Z-score heme from (Dali one identity DyPs has low subunit of each alignment ratio, stoichiometric pairwise antiparallel 1 four-stranded Structure-based : a domain. 1 of the with consists accordance domain In Each cation. domains: domain. into twoferredoxin-like C-terminal larger divided is have a β they and though DyP protomer even domain superfamily N-terminal Thebacterial new an a [10]. constitute identity to proposed sequence been significant have no proteins (like) Clds and DyPs fore, an share 8 setsrone by surrounded -sheet DyP2 SCO7193 BtDyP tteratv ie h otciia eiusaeteaillgnsfrtehm.I l ys h eeio is iron heme the DyPs, all In heme. the for ligands axial the are residues critical most the site, reactive the At ysaevr ifrn rmcasclprxdss hc areprimarily which peroxidases, classical from different very are DyPs hnadLi and Chen vrl tutr n eeevrneti atra ys a,() n c ersn vrl tutrso A- of structures overall represent (c) and (b), (a), DyPs. bacterial in environment heme and structure Overall α + β erdxnlk odta eebe h etaysrcueo hoiedsuae Cd)[1.There- [61]. (Clds) dismutases chlorite of structure tertiary the resembles that fold ferredoxin-like 75iv2 sp. Amycolatopsis coelicolor Streptomyces VPI-5482 taomicron thetaio Bacteroides MR-1) (strain ε tmo rxmlhsiiei -emnldmi,adteN the and domain, C-terminal in histidine proximal a of atom α hlcs h osre oooyi ahdmi a elc h euto eedupli- of gene result the reflect may domain each in topology conserved The -helices. - C B B Mn) (heme, 4G2C 4GU7(heme) 2GVK (apo) 2HAG α hlcs(cyan), -helices K7N5M8 Q9FBY9 Q8A8E8 α hlclpoen 6] l DyPs All [61]. proteins -helical β set(aet)a elas well as (magenta) -sheet δ tmo h rxmllig- proximal the of atom predicted) (PISA Dimer (crystal); Monomer Dimer Hexamer β setcores -sheet EGRUYTER DE Automatically generated rough PDF by ProofCheck from River Valley Technologies Ltd oeDP lohv nadtoa itlcanl u ti eaieynro,teeoecnol accommodate only can therefore narrow, relatively 9). is (Figure it DyPs characterized but all channel, in distal observed additional is proposed it an is as have channel substrates, also This small DyPs orientation. for outward Some route adopt access heme substrate of common moieties a acid be propionic to two the that fact the from incorporation, heme only not [43]. to turnover contribute to catalytic speculated the is also and domains, but two the of movement relative the the bridges from that 222 loop residue flexible include long 200 loop a residue by the has include surrounded EfeB, It usually In insertion. is domains. heme DyPs C-terminal in in and involved side pocket likely N- except binding are heme binding factors the heme other that upon that found suggesting change been [38], little residues revealed several 2IIZ) in code rotation chain (PDB holo-TyrA and 2HAG) code structure (PDB X-ray TyrA and crystallization protein as state native [67]. artifacts oxygen the an create represent to may bounded not EfeB determination may in iron presence heme Their species. the varying while [43]. by [28], occupied molecule species solvent is iron-coordinated face (f)). an distal had the and heme on DypB (e), site site. The coordination active (d), sixth the 8 the however, in structure, (Figure crystal heme conformation In forms the hemes. and bent position Å), a to 4.3 helps in (~ arginine D iron the pyrrole heme that on the suggests functions. to moiety conformation additional residue propionate particular suggests closest This the arginine arginine the with is conserved conserved bond arginine the the hydrogen the of structures, a that position DyP indicating available The I, the [66]. on compound catalysis Based of in DyP role formation In essential the debate. an O prevented under plays during mutation also peroxide di- the R244L charged is play negatively although the to arginine the likely enzyme, conserved RHA1, stabilize most the wild-type the to is of proposed as residue role is aspartate R329 The the efficiently Indeed, DyPs. as DypB [66]. in just with reduced roles dramatically I study vergent was compound mutation I of compound the However, of pH formation [8]. stability have the acid DyPs catalyze bacterial aspartic can all the mutant that of cytochrome fact carboxylate in the the by histidine of com- from supported distal forming pKa also the to the is of prior around notion that peroxide optima This to the [65]. equivalent from chloroperoxidase proton is in a role glutamate accepting This by [13]. catalyst I acid-base DyP pound an For as (e)). function and to (d), proposed H (c), with 8 reactivity (Figure lost phenylalanine D171N a and loops. arginine three an the and respec- rotation) cyan, 90° and by green (related in orientations two colored are with residues model TcDyP catalytic the proposed of the presentation and Surface heme (b): The tively. situated. is 276 H312 of axial loops two proposed and domains, two the necting 9: Figure proximal histidine of the role the II. fill compound to of stage the to otherresidues catalysis allow the may out carry region to H312A this in located is in H312 flexibility the Indeed, structural [14]. high region The the that in suggesting residues very other (d)), short have the a 6 by mutant on rescued (Figure H312A TcDyP-II) partially was and the H312A TcDyP-I, (TcDyP-0, and of with TcDyP function intermediates state the wild-type resting all The found the for cycle. to those features catalytic II to spectral a compound comparable similar complete from activities reduced cannot the be H312A with cannot II Hence, mutant and HQ. the I However, compound enzymes. form wild-type to the able in was mutant H312A the kinetics, GRUYTER DE nEe,tehm sstae tteedo rpoaecanlo h rxmlsd 4] h aecomes name The [43]. side proximal the on channel propionate a of end the at situated is heme the EfeB, In apo- of alignment Structural DyPs. in cavity buried deeply the into incorporated is heme how unclear is It penta-coordinated high-spin, contain DyPs state resting that shows solution in DyPs of study Spectroscopic aspartate, an including residues conserved highly three have DyPs bacterial heme, the of face distal the On .jostii R. h cy oe tutr.() ibnpeetto fteTDPmdlicuigalo f200 of loop a including model TcDyP the of presentation Ribbon (a): structure. model TcDyP The α hlxbtentolrelos(G276 loops large two between -helix H1sgetdta h osre satt sntesnilfrprxds ciiy h D153A The activity. peroxidase for essential not is aspartate conserved the that suggested RHA1 – 229, both at the confluence of the two domains (Figure 9). The flexibility of thisloopcomes 9). Theflexibility (Figure twodomains the of confluence the at both 229, 2 O 2 sidctdb VVssetocp 1] h ovre satt eiu is residue aspartate conversed The [13]. spectroscopy UV-Vis by indicated as – 1(elw n 317 and 311(yellow) – 31adH317 and A311 – 2 mgna lnigteshort the flanking (magenta) 329 – – 39 ntehmlg oe Fgr )[14]. 9) (Figure model homology the in P329) 4 4] hl nTDP h qiaetloop equivalent TcDyP, the in while [43], 243 Dec1 – Ofission [13]. For DypB from For [13]. Ofission from .cucumeris T. c eoiae[3 rta of that or [63] peroxidase Dec ,tegaiieof guanidine the 1, α e1 h mutant the Dec1, hlxweethe where -helix hnadLi and Chen – 2 rd con- (red) 229 .jostii R. 9 Automatically generated rough PDF by ProofCheck from River Valley Technologies Ltd steoiainst ttebgnigo nLE aha.Tetroe novn h RTmcaimshowed mechanism Trp377 LRET employs s the mainly involving s turnover enzyme 200 The pathway. the LRET of 19, an turnover of Blue a beginning Reactive the of at degradation, oxidation site the oxidation from lignin the In DyP as Kraft wood. the on of For grows study the center. systematic that and the surface heme fungus protein from common buried the comes between evidence deep network Stronger relay [28]. the radical site a from active employ may occluded DypB that are suggests analysis they structural midway since [69]. a dyes, peroxidase [7]. since di-heme synthetic heme a DyP2, the or in for from mechanism away proposed 16Å the been by ~ suggested are therefore as that has relay residues mechanism electron acid facilitate (LRET) glutamic Mn can transfer three Tyr188 the manganese of electron carboxylates DyP2, fungal distance by in long in held contrast, is A found By it those [31]. as iron residues to Mn the acidic similar although by typical site, distance the Fe-heme a of the study shows heme, instead in Kinetic oxidized species the probably polymer. from is of the away It [68]. 4.2Å peroxidases is theinterior manganese bound canaccess Mn the employ can DyPs that C-type mediator and B- diffusible that a as degradation lignin glvnli fe i aswe rw nmnmlmdu upeetdwt .%wetsrwlignocellu- straw wheat 2.5% of with strain produced supplemented different medium also a minimal In but on loses. grown degradation, when lignin days six for after vanillin responsible mg/l only not from were product vanillin peroxidases the The [77]. straw soil pro- wheat Gram-positive the chemical from In over monomers. advantage compatible distinctive process into a depolymerized is bacterium be to This needs products. lignin useful which in into cesses, lignin of conversion direct permitting com- These compounds. 76]. mono-aryl [75, give molecules to aromatic pathways give dedicated of the to their plethora by by degraded a mediated are give are pounds to They peroxidases etc. Mn na- acid, In or ferulic [73]. lignin include products extracellular aromatics value-added These by into [74]. degraded them is transforming lignin and aromatic molecules ture, industry. for small petroleum feedstock into the alternative depolymerization in an process lignin become BTX to the value from expected the derived is but currently byproduct, Lignin are annually low. lignin which lignin use very of to of is most ways tons approach chemicals, easiest million the this 60 has of from about It one industry. energy generate is biofuel will of combustion plant the industry lignin in of bioethanol from produced US production 25% Power be the [1]. will comprises manufacture 2022 lignin paper by which of and that cellulose amounts pulp estimated larger from after been even byproduct Potentially a biopolymer process. as abundant Kraft generated are the most lignin via of second quantities the Large average. is on biomass walls cell in Lignin chemicals fine and valorization Lignin 1 standard applications. in biotechnological yield for tools high attractive pro- in are via synthesized DyPs optimize to bacterial be with together, ligninmodel easier can integration are dyes and facile and they proteins, permitting engineering, prokaryotic al- conditions, tein As have recalcitrant conditions. acidic enzymes acidic including under under characterized of substrates, activities hydrolysis Many lignocellulose maximal display activities. an array provide novel also have They metagenome toward potentially compounds. activities and that efficient sequencing DyPs shown next-generation bacterial over ready in of advantages Advances many variety peroxidases. offering vast by a classical biocatalyst and promising DyPs a as fungal emerge peroxidases dye-decolorizing Bacterial opportunities Biotechnological 6 is mechanism another dyes, or polymer lignin as such substrates bulky needed. handling In substrates. smaller even 10 – 1 [20]. RTmcaimmyas lya motn oei y aayi o uk usrtssc slignin as such substrates bulky for catalysis DyP in role important an play also may mechanism LRET A nutilboehooyalw nerto flgi eoyeiainwt ute rnfrain thereby transformation, further with depolymerization lignin of integration allows biotechnology Industrial involves which valorization, lignin to contributions great make to expected is biotechnology Industrial Mn of mechanism the to insight provides study Structural hnadLi and Chen β ktaii cda h omnitreit eoejiigtecnrlmtbls ..teTAcycle TCA the i.e. metabolism central the joining before intermediate common the as acid -ketoadipic .jostii R. H1 ncigottevnli eyrgns eeealdvnli rdcindirectly production vanillin enabled gene dehydrogenase vanillin the out knocking RHA1, – 1 rvn t motneoe h iethm cesrue hc hwdatroe f20 of turnover a showed which route, access heme direct the over importance its proving , β ay tesvateprxdto ecin[] h uatsri rdcdu o96 to up produced strain mutant The [6]. reaction peroxidation the via ethers -aryl .jostii R. β β ktaiaeptwy i ihrpooaehaebac rctco branches, catechol or branch protocatechuate either via pathway, -ketoadipate Ay tes ihnl,day rpns ioeios hnlomrns and phenylcoumaranes, pinoresinols, propanes, diaryl biphenyls, ethers, -Aryl H1 rmtcdcroyi cd a epoue ietyfo innby lignin from directly produced be can acids dicarboxylic aromatic RHA1, 2+ /Mn 3+ necneso omdaelgi xdto.I DypB-N246A, In oxidation. lignin mediate to interconversion 2+ xdto.Mnaeepasaciia oein role critical a plays Manganese oxidation. .coli E. 2+ xrsinsses[70 systems expression sdrcl oriae ysolvent by coordinated directly is 2+ antb xdzddirectly oxidized be cannot uiuai auricula-judae Auricularia – EGRUYTER DE 2.Taken 72]. a , Automatically generated rough PDF by ProofCheck from River Valley Technologies Ltd involves the typical intermediates at different oxidation stages. Kinetic study contributes to the understanding that mechanism contributes same study and physiological the Kinetic stages. share oxidation they specificities different peroxidases, at substrate classical intermediates diversified from typical distinct highly the involves structurally with are peroxidases they Although heme roles. novel are DyPs Bacterial perspectives and Conclusions 7 offer. may DyPs that advantages im- the upon explore enzymes to work other more in encourage destabilized should preserved often result PpDyP was This immobilized however 88]. the which [87, environment, that mobilization revealed heme analysis of spectroscopic activ- integrity Re- electro-catalytic Raman efficient structural enzymes. have [86]. asprokaryotic to peroxide found was the the advantage and towards electrodes, ity Ag all on offer immobilized was horseradish DyPs Historically, PpDyP bacterial B-type H cently, electrode. peroxidase, for the horseradish enzyme to and alternatives popular enzyme As most the between the directly is determina- place peroxidase amperometric takes for transduction basis the signal provide the current electric with H Fe(III) of to tion Fe(IV) oxidized the of reduction in unique deferrochelase be a can as role acquisition their [43]. iron development DyPs, in from drug bacterial role arisen antimicrobial known key for few often a very plays has For EfeB crisis organisms. critical. eukaryotic health and higher bacteria. public in in found a absent predominantly are are as DyPs They C-type critical and B-, is A-, pathogens. therapeutics antibiotic-resistant surrounding antimicrobial issues novel of exploration The applications industrial potential Other 3 efficiency catalytic the RB5, dye recalcitrant a of 10 oxidation × the 1.2 as In high [26]. as reached azoreductase and laccase including biological for opportunity great a presents wastewater en- Treating the components. decolorization. into major food discharge the cosmetics, its are textiles, dyes before of thraquinonic treated 10 manufacture be over the year to in Every needs vironment. wastewater used dye-contaminated are The that pharmaceuticals. xenobiotics and stable chemically are dyes Synthetic treatment wastewater in decolorization Dye source. 2 carbon a and as substrate, p-coumarate the using as mode fed-batch lignin in use of g/l could 13.5 insertion strain of and yield engineered CatBC muconate The and highest [80]. the PcaHG was Dmp-KLMNOP reached encoding strain and genes this AroY of production, encoding muconate deletion genes involving enhance To manipulation [79]. genetic biomass by enriched improved lignin pretreated from (PHA) organ- noates depolymeriza- same lignin from the the aromatics by diverse join transform to used can tion which be repertoire can metabolic diverse which a bacterium with intermediate, Gram-negative organism products. common useful a produce give to to ism which catabolized in strategy, are funneling biological aromatics a diverse by overcome be the can problem This biotransformation. via product neous [78]. cleavage aryl in DypB and 2,3-dioxygenase DypA protocatechuate with or work to (LigAB) 4,5-dioxygenase (PraA) protocatechuate of genes exogenous introducing GRUYTER DE noeogns hudpoiemn pin o y eooiainaddtxfcto [84]. detoxification and decolorization dye for options enzymereactions many of multiple provide should and integration organism con- DyPs, one ofnew two involve in rendered may [83]. Discovery further RB5 dyes organism of industrial decolorize same decolorization efficiently the the in that from reactions suggest peroxidase enzyme results secutive versatile These a [82]. with TcVP1, colorless peroxidation products Adding the red-brown acid. of Analysis phthalic [36]. and degradation pounds RB5 for studied been DyP only has pathway degradation The putida P. nteoiaino eoiaeb yrgnprxd,teoiainsaeo ei hne rmIIt V Direct IV. to III from changed is Fe of state oxidation the peroxide, hydrogen by peroxidase of oxidation the In enzymes dye-degrading other than activities decolorizing higher 40-fold to up shown have DyPs Bacterial homoge- producing to barrier a presenting thus mixture, heterogeneous a gives depolymerization Lignin Dec1 2 E 4adBDPfrom BsDyP and 94 MET hwdta h rdcsfo B nlddtremjrpout,icuigtordboncom- red-brown two including products, major three included RB5 from products the that showed O 2 ocnrto 8] nsno eeomn,teprxds simblzdo h lcrd,s that so electrode, the on immobilized is peroxidase the development, sensor In [85]. concentration β ktaiaeptwy tsoe h blt opouemdu hi eghpolyhydroxyalka- length chain medium produce to ability the showed It pathway. -ketoadipate 7 M .cucumeris T. 5 – 1 oso yswr eesdit atwtrsra 8] fwihaoadan- and azo which of [81], stream wastewater into released were dyes of tons s – .subtilis B. 1 oeDP aebodsbtaeseiiiis o xml,PDPfrom PpDyP example, For specificities. substrate broad have DyPs Some . e .Teeaeol iie ubro nw nye htcan that enzymes known of number limited a only are There 1. Dec aesmlratvte oad z n nhaunncde [26]. dyes anthraquinonic and azo towards activities similar have 2 O 2 esrdvlpetbcuei sawl-tde enzyme. well-studied a is it because development sensor .putida P. T40i aua aromatic-catabolizing natural a is KT2440 .coli E. 4] tmysrea target a as serve may It [42]. hnadLi and Chen 11 Automatically generated rough PDF by ProofCheck from River Valley Technologies Ltd 1]Ce ,Srsh ,JaK ta.Caatrzto fdedclrzn eoiae(y)fo hrooopr uvt eel unique reveals curvata Thermomonospora from (DyP) peroxidase dye-decolorizing of Characterization al. et KM Jia R, Shrestha C, peroxidase Chen heme [14] novel a represents per-oxidase, dye-decolorizing unique DyP, a M. Shoda T, Sato A, Ichiyanagi R, Muramatsu Y, peroxidase, Sugano dye-decolorizing [13] unique a of oryzae Aspergillus in expression heterologous Efficient ShodaM. K, Sasaki R, of Nakano Y, decolorization Sugano in [12] involved 1 dec candidum Geotrichum from peroxidase novel a of characterization and com- Purification families ShodaM. enzyme SJ, heme Kim microbial [11] 3 EfeB: and DyPs, dismutases, Chlorite JL. DuBois CM, Wilmot BR, Streit RC, Kurker B, Goblirsch [10] M. Ayala E, Torres [9] superfamilies, peroxidase heme four of evolution Independent al. et I Schaffner S, Hofbauer M, bacterium, Zamocky lignin-reactive [8] a from peroxidase dye multifunctional a of characterization and peroxi- Identification lignin MC. a Chang T, as Barros RHA1 ME, jostii Brown Rhodococcus [7] from DypB of Identification TD. Bugg LD, Eltis R, Singh EM, Hardiman JN, Roberts M, bac- Ahmad unsequenced [6] from enzymes heme of characterization and Discovery MC. Chang AT, Iavarone TG, Nakashige MC, formation, Walker bio-product ME, and Brown degrada-tion [5] lignin in bacteria for role emerging The R. Singh EM, Hardiman M, Ahmad TD, the Bugg of [4] aspects enzymatic and chemical, micro-bial, lignocellulosics: of Biodegradation biorefinery, al. the et in FJ processing Ruiz-Duenas lignin M, improving Speranza AT, valorization: Martinez Lignin [3] al. et MJ Biddy GT, Beckham AJ, Ragauskas [2] D. Johnson JJ, Bozell JF, White JE, Holladay [1] References 978 isbn (2016), Gruyter De Biomaterials. Luque/Xu, in: available also is article This EPA. US Acknowledgement the or States United Protection the those Environmental of are States those expressed represent views United necessarily The the capacity. not governmental do or any and Government in only work States authors this United the doing of the not are of authors product the and a Agency, not is work This Disclaimer from be sequences to metagenome expected DyPs. in is peroxidase found a be of to performance by expected operational improved are in the diversity DyPs development, the process unique For on more environments. depends Many diverse biocatalysts DyPs. right bacterial the of Finding pool valorization. the lignin or degradation dye context. synthetic to genomic ing related and necessarily property not biochemical are their DyPs by these shown of as roles activity physiological peroxidase The property. their biochemical of terms in acterized may deserves involve which in it Therefore found substrates. Themechanism, bulky activity of Mn oxidation degradation. study. the The comprehensive onlignin for DyPs. important more and bacterial activity unique few is their transfer, a for electron range aspartate, in significant long an study is charge including DyPs the catalysis, unique, C-type on base acid/ and are based be B- heme positioning to of speculated heme been side even have distal catalysis or in the stabilization, roles active at Their the phenylalanine. residues a In acid and catalysis. arginine, amino enzyme an in conserved residues the acid DyPs, amino of of site roles and selectivity, substrate mechanism, catalytic of 12 substrate exhibiting subtilis fromBacillus peroxidase dye-decolorizing A Y. Um Y, Kim HM, Woo G, Gong K, Min [15] aayi rpriso -yeDyPs, A-type of properties catalytic peroxidases, classical of histidine distal the replaces ASP171 family: 1, Dec candidum Geotrichum DyP, of dyes, superfamily, structural CDE the prise 108 Biol Chem ACS dase, degradation, lignin microbial to application teria: Biotechnol lignin, of attack fungal 2007. Energy, of Department US Lignin. fromBiorefinery includ- applications industrial in biocatalysts for search the in found char- been well have DyPs are of them numbers of Increasing number limited a only recognized, well is DyPs bacterial of diversity the Although eprtr o ysadbt-te inndimer, lignin beta-ether and dyes for temperature – hnadLi and Chen 19. plEvrnMicrobiol Environ Appl Biochemistry 01 2 394 22, 2011, , nvitro in 02 ,2074 7, 2012, , ictlssbsdo eeprxdss eoiae sptnilidsra biocatalysts industrial potential as peroxidases peroxidases: heme on based Biocatalysis 01 0 5096 50, 2011, , vlto.Tgte,teeatvte hudeal h rcia plcto ihbacterial with application practical the enable should activities these Together, evolution. IntMicrobiol – 400. 99 5 1029 65, 1999, , – 81. – 107. 05 ,195 8, 2005, , ilChem Biol J plEvrnMicrobiol Environ Appl MlBiol JMol o au de hmcl rmBiomass from Chemicals Added Value Top – 35. 01 0,379 408, 2011, , 2015, , – 204. mCe Soc Chem Am J c Rep Sci 290 23447 , 05 ,8245. 5, 2015, , 00 6 1754 66, 2000, , – 98. – 01 3,18006 133, 2011, , 63. ilChem Biol J – 8. 07 8,36652 282, 2007, , oueI:Rslso cenn o oeta Candidates Potential for Screening of Results II: Volume . – 9. – e ok Springer-Verlag, 2010. York: New . 8. – rhBohmBiophys Biochem Arch 3 – 11 Science – – eedn optimum dependent 034230 04 4,1246843. 344, 2014, , – 7. EGRUYTER DE 05 574, 2015, , urOpin Curr Automatically generated rough PDF by ProofCheck from River Valley Technologies Ltd 4]CnrrsH on S cahL ta.Caatrzto faMcbceimtbruoi aooprmn n t oeta cargo potential its and nanocompartment tuberculosis Mycobacterium a of Characterization al. et LM McMath MS, nanocompartment, Joens a H, form Contreras to [48] DypB peroxidase and encapsulin RHA1 jostii Rhodococcus of vitro in Assembly TD. Bugg peroxidases, R, dye-decolorizing Rahmanpour of [47] palette multihued The LD. translocated Tat-dependently Eltis of R, class Singh novel [46] a reveals coli Escherichia from YcdB T. Bruser H, Lilie U, heme Lindenstrauss a A, Schierhorn not oxidase, A, porphyrinogen Sturm a [45] as functions YfeX protein coli Escherichia The al. et L divergent Daugherty plays AN, ASP235 Septer O157: HA, coli Dailey Escherichia [44] from EfeB/YcdB of features biochemical and structure Crystal al. et Z Wang Q, Du oxida- X, and Liu catabolism, [43] motility, flagellar for genes regulates pH JL. Slonczewski stress, oxidative M, severe Radmacher SS, under Bondurant mechanisms E, defense Yohannes frontline LM, of Maurer Coordination [42] al. et CR Busch PT, Van basid- A, Kaur the [41] from oxidase phenol peroxide-dependent hydrogen novel of cloning cDNA and Isolation T. Kudo nonphe- M, oxidize Ohkuma T, auricula-judae Johjima Auricularia [40] fungus jelly the of peroxidases DyP-like M. Hofrichter R, Ullrich M, Pecyna peroxi- C, dye-decolorizing Bobeth novel C, a Liers in [39] binding heme of characterization structural and Identification al. et SS Pseudomonas Krishna from R, peroxidase Joseph DyP-type novel C, Zubieta a of [38] characterization molecular and Identification B. Zheng J, Yang H, Yuan B, Li unique C, a Liu J, by catalyzed Li dye [37] anthraquinone an of pathway Degradation M. Shoda M, Hirai H, Aoki K, Tsuchiya Y, Matsushima Y, intact, Sugano skeleton tetrapyrrol [36] keeping by heme from iron capture Bacteria C. Wandersman alcohol, N, veratryl P, Lange by Delepelaire Mediation G, peroxidase. Heuck lignin S, by Letoffe acid [35] 4-methoxymandelic of fungus white-rot Oxidation D. the Ma from M, peroxidase Tien versatile [34] new a by binding manganese(II) of study NMR al. et AT Martinez S, Camarero L, Banci complexes, [33] manganese with reaction The peroxidase. manganese of analysis Kinetic M. Tien lignolytic KA, a Johnson from IC, peroxidase Kuan a [32] DypB, of activity manganese-oxidizing Improved LD. Eltis ME, Murphy JF, Kadla W, Qin JC, Grigg R, Singh species [31] Bjerkandera by produced isozyme hybrid peroxidase peroxidase-lignin manganese novel a of Characterization JA. of Field mutants T, site Mester binding [30] manganese(II) of Characterization MH. Gold TM, Loehr J, Sun MB, Mayfield M, Someren Kusters-van jostii K, Rhodococcus Kishi from [29] peroxidases dyedecolorizing of Characterization LD. Eltis TD, Bugg ME, Murphy JC, Grigg R, Singh JN, Roberts [28] manganese by compounds model lignin ether beta-aryl arylglycerol phenolic of Oxidation MH. Gold HE, Schoemaker H, Wariishi U, Tuor MET94: [27] putida Pseudomonas and subtilis Bacillus from peroxidases dye-decolorizing New LO. Martins V, Brissos S, Mendes A, Santos optimiza- [26] medium by lavendulae Streptomyces from peroxidase lignin and laccase of production simultaneous monolignols, the of Improving potentials D. oxidation Jing and [25] energies dissociation bond on study theoretical A Q-X. Guo L, Liu Y, S-W, Fu strain Luo sp. K, Anabaena Wei cyanobacterium [24] the from peroxidase novel a of characterization Molecular al. et N Hashimoto T, a Kamiike substrates: HJ, potential Ogola redox [23] low for sites oxidation Two FJ. Ruiz-Duenas AT, Martinez MJ, Martinez A, Romero inter- MJ, substrate Mate peroxidase: M, dye-decolorizing Morales potential [22] high-redox fungal a of structure crystal First al. et R Ullrich C, site- Liers and E, spectroscopic Strittmatter computational, [21] a peroxidase: dye-decolorizing in radical surface Catalytic al. et M Canellas R, Pogni D, Linde [20] peroxidase dye-decolorizing auricula-judae Auricularia of toolbox The al. et C Liers K, Serrer E, Strittmatter Thermobifida [19] from peroxidase heme-containing extracellular and robust A MW. Fraaije RT, Winter DE, database, Pazmino families Torres protein E, the Bloois Pfam: van al. [18] et J Clements A, Bateman RD, poly- Finn and [17] Mn(II) of Oxidation Pf-5: fluo-rescens Pseudomonas from peroxidases Dyp-type of Characterisation TD. Bugg R, Rahmanpour [16] GRUYTER DE 4]Ste ,Berne ,GtanSe l tutrlbsso nyeecpuainit atra nanocompartment, bacterial a into encapsulation enzyme of basis Structural al. et S Gutmann D, Boehringer M, Sutter [49] proteins, J FEBS hemoproteins, dechelatase, processes, enzyme-catalyzed different in roles K-12, coli Escherichia in stress tive Microbiol Appl albuminosus, Termitomyces iomycete dyes, potential high-redox and compounds model lignin nolic TyrA, dase, PKE117, aeruginosa 1, Dec cucumeris Thanatephorus from DyP peroxidase A S U Sci Acad Natl eryngii, Pleurotus 20064 bacterium, manganese, of absence the in BOS55 strain peroxidase, manganese RHA1, compound, model 95. alpha-carbonyl an of cleavage oxidative chrysosporium: Phanerochaete from peroxidase applications, biotechnological towards tion, THEOCHEM Structure: Molecular of 7120, PCC peroxidase, versatile eryngii Pleurotus on study crystallographic and kinetic, mutagenesis, directed transfer, electron long-range and sites action study, mutagenesis directed sites, substrate-interaction potential superfamily, peroxidase bacterial a of prototype as fusca Dyp1B, by lignin meric Biol 08 5 939 15, 2008, , irsu Technol Bioresour 03 8,2097 280, 2013, , – Biochemistry 70. ilChem Biol J plEvrnMicrobiol Environ Appl Proteins C hmBiol Chem ACS MBio ilChem Biol J – 09 0,11719 106, 2009, , 01 ,e00248 2, 2011, , ilIogChem Inorg Biol J 47. 07 9 234 69, 2007, , 01 0 5108 50, 2011, , plBohmBiotechnol Biochem Appl 04 8,18279 289, 2014, , 00 0,7592 101, 2010, , – rhBohmBiophys Biochem Arch 104. 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Martins CA, Viegas JH, Leitao CG, Ramos A, Farinha S, Mendes [84] dyes textile of decolorization the for Bioremediation GM. two Gubitz of A, action Kandelbauer concerted [83] the by 5 blue Reactive dye anthraquinone the of decolorization Complete dyes, M. azo Shoda of Y, degradation Matsushima Y, microbial Sugano the [82] in aspects applied lignin, and from Basic production A. acid Stolz Adipic [81] al. et CW Johnson MA, Franden DR, catalysis, Vardon chemical [80] and funneling biological integrated through valorization Lignin al. et MT Guarnieri DR, RHA1 Vardon jostii JG, Rhodococcus Linger in [79] acids dicarboxylic aromatic to lignin of conversion Biocatalytic TD. P, Bugg P, Law Mines vanillin M, to Gomis lignocellulose Z, Mycroft of conversion [78] the chemicals: high-value to lignin down Breaking al. et M Ahmad EM, self-identity, Hardiman of PD, biology Sainsbury the [77] and pathway beta-ketoadipate The RE. 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Poulos MH, Gold UV- M, by Sundaramoorthy analysis [68] proteins: heme crystalline of reduction Cryoradiolytic I. Schlichting RL, Shoeman C, Schulze-Briese but K, arginine Kuhnel peroxidase: T, dye-decolorizing Beitlich B-type [67] of residues pocket heme Distal LD. Eltis ME, Murphy Z, Armstrong JC, Grigg R, Singh [66] peroxidase heme a chloroperoxidase: of structure crystal The TL. Poulos J, Terner M, Sundaramoorthy [65] perox- c cytochrome in effects pull and push the of analyses NMR 15N and 13C Paramagnetic H. Fujii KG, Welinder H, Wariishi D, cou- Nonaka and structure, [64] electronic potential, reduction the controls peroxidase c cytochrome of triad Asp-His-Fe The DE. McRee DB, Goodin 3D, [63] in mapping conservation server: P. Dali Rosenstrom enzyme, L, classic Holm a [62] of view con- modern a a with peroxidase: fold Horseradish beta-barrel NC. 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