to the studies on degrading , among which ar which among enzymes, degrading on studies the to Introduction of aromaticcompounds Intradiol –enzymesinvolved indecomposition can be also found in the corners of opposite walls. Between walls. opposite of corners the in found also be can 50Å. of diameter the α having sheath hollow the making symmetry oligomer structure and they are arranged along the axis of tetrahedron yrxqio 12doyeae cmoe of composed 1,2-dioxygenases hydroxyquinol ai fr iiig ixgnss rm hs ru it te following: the of into composed 1,2-dioxygenases catechol group this the The from formed dioxygenases sequence line. dividing acid for evolutionary amino basis and same structure spatial the of (III). from analysis originate nonheme with probably enzymes of They family small the a in is It compounds pathway. aromatic of decomposition system, the aromatic the initiating of atoms carbon hydroxylated two between o aehl ixgnss Dsie ifrn sbnt composition, subunit different catalytic domainsofintradioldioxygenasesareformedsimilarly. Despite dioxygenases. catechol to 3,4-dioxygenases composed of different numbers of numbers different of composed 3,4-dioxygenases h ( the transformation of protocatechuic acid into 3-carboxy- into acid protocatechuic of transformation [4, 5]. ligands detached t its gave substrate attached Tyrosinethe and 447, hyd of separation the with associated was substrate the that showed 3,4- protocatechuate of -subs of structure the on tests The function. is site active the of composition The plane. axial p Tyrosine whereas in plane, the equatorial 447 both and H of tops the at Tyrosine molecules 460 and 408, group are Histidine hydroxy a 5 to linked is format atom bipyramidal trigonal the e In four ligands. with protein bound geometry coordination bipyramidal and is composed of two different types of subunits – subunits of types different two of composed is and structure oligomer the by characterised is enzyme This [1,6,7]. acid ( chlorophenol as: intermediates hyd valuable in also it results obtaining aromatic such polycyclic and biphenyls compounds nitrophenols, degradation aromatic the provide degradable only not does participa the dioxygenases with cleavage ring The [3]. extradiol cleava ring the of regiospecificity the on depending fo two into classified are they and oxygen attac molecular Suc of result a [1,2]. as ring a of meaning opening the key catalyse a have dioxygenases cleavage been has attention considerable compounds, aromatic cis, cis cis, subunits are arranged in proximity to the peaks of two axes; they they axes; two of peaks the to proximity in arranged are subunits Intradiol dioxygenases catalyse the opening of the aromatic ring aromatic the of opening the catalyse dioxygenases Intradiol pr biodegradation in interest large a of era the In In the of intradiol dioxygenases, there dioxygenases, In site of the active intradiol Protocatechuate 3,4-dioxygenase is the enzyme that catalyses the the catalyses that enzyme the is Protocatechuate 3,4-dioxygenase αβ Please citeas:CHEMIK2012, Danuta structures of intradiol dioxygenases Modern research methods for determining in Katowice – Department of Biotechnology, Faculty of Biology and Environmental Protection, University of Silesia -muconic acid and 3-carboxy- and acid -muconic Fe) n structure. nr 12/2012 • tom66 OCEZŃK, aazn HUPERT Katarzyna WOJCIESZYŃSKA, β subunits combine protomers forming the the forming protomers combine subunits cis, cis cis, 66, α subunits, protocatechuate protocatechuate subunits, 12,1346-1351 -muconic acid). -muconic for organic syntheses syntheses for organic α closely related to its its to related closely subunits, similarly similarly subunits, hing two atoms of of atoms two hing wo protons to the the to protons wo istidine 462 in istidine the ttached to ttached Fe (III) is iron in trigonal ge: intradiol and and intradiol ge: tion of intradiol intradiol of tion ion, the central central the ion, α αβ roxy group and and group roxy cis, cis cis, rocarbons, but but rocarbons, llowing groups groups llowing and trate complex complex trate attachment of of attachment subunits and subunits yramids [2]. [2]. yramids omatic ring- omatic h enzymes enzymes h of uneasily uneasily of ndogenous ndogenous ocesses of of ocesses directed directed β -muconic forming forming s and and s α ortho and

- h hlcl onco peet t h sbnt bounda subunit the at present connector helical the to similar is structure whose domain catalytic the α been closely investigated so far [5, 6, 9]. 6, [5, far so phospho investigated closely of been role The attached. being is phospholipid cla this both of the sub regarding dioxygenases other intradiol Dioxygenases helices. 5 making residues ca. of consists domain N-terminal doma dimerisation. in terminal the and dioxygenases, protocatechuate two into coiled and acids amino 300 ca. of composed ring into ring enzymes [EC 1.13.11.1]. These enzymes cleave the catechol aromatic a pieceofpaperwhenfoldedinhalf[2,5,6]. tosimilar is It structure. closed the into coiled and twisted chains, 8 its chlorinatedandmethylatedforms[7÷10]. and methylcatechol,lessoftenchlorocatechol Theyare: subclasses oftheseenzymesaredistinguished. rnfrain no 3-hydroxy- into transformation to catechol dioxygenase, which is related to their their to related is which dioxygenase, catechol to of ca. 200 amino acid residues, while residues, acid amino 200 ca. of subunits are homologous towards each other.each towards homologous are subunits β of conformation the has structure secondary The residues. acid amino ixgnss E 11.13] Te ctls hydroxy catalyse They 1.13.11.37]. [EC dioxygenases of 110x50x50 of Å. 110x50x50 Its and structure compositi subunit d hydroxyquinol simplexNocardioides for described was structure spatial the attachment of the dianonic substrate were observed. This led to the the dissociation of ligands coordinated with iron from the active site and deprotonation of both hydroxy groups of the substrate. Simultaneously, group, and the second to hydroxy tyrosine to in one the – protons axial two position, gave which substrate caused The the site. active the to and spectroscopicproperties. biochemical of basis the on as well as complexes enzyme-substrate and 1,2-dioxygenase catechol and 3,4-dioxygenase cleavage protocatechuate of ring structure spatial the of aromatic analysis the of basis the intradiol on suggested was of mechanism The investigated. 8]. [5, site active the of part upper the in Phe1 Pro110, attach for openings big Val251) and Arg218, Pro200, Gly109, Phe108, Val107, th in Asp83, residues (Leu80, acid amino specific have dioxygenases dioxygenas catechol with affinity close that Despite OUE, agraa INK Usua GUZIK Urszula SITNIK, Małgorzata KOCUREK, uuis bt o wih oti F(I) . Fe(III) contain which of both subunits, subunits, near the peak of the symmetry axis, there is an active site. The β Hydroxyquinol 1,2-dioxygenases belong to 3 to belong 1,2-dioxygenases Hydroxyquinol Catechol 1,2-dioxygenases belong to the widely described class of aehl ixgnss r hmdmr o to identic two of homodimers are dioxygenases Catechol as well as catechol decomposing dioxygenases chlorocatechol – II I – catechol dioxygenases catalysing the decomposition of catechol The process of ring cleavage began from substrate attachment attachment substrate from began cleavage ring of process The fully been not has cleavage ring of mechanism intradiol The bre cntttd of constituted -barrel cis,cis -muconic acid. Regarding the catalysed substrate, two two substrate, catalysed the Regarding acid. -muconic strain 3E. It is a homodimer having the dimensions β set tutr ta i cmoe of composed is that structure -sheet i, cis cis, α subunit is composed of 230 of composed is subunit -muconate. The model of of model The -muconate. β subunit is composed is subunit rd group of intradiol intradiol of group es, hydroxyquinol hydroxyquinol es, unit structure and unit structure on on ( ing the substrate substrate the ing 100 amino acid acid amino 100 Each subunit is is subunit Each ss differ from from differ ss ries, to which which to ries, ioxygenase of of ioxygenase lipids has not not has lipids α ls affinity. close eir structure structure eir the core of of core the 2 ) ) are similar in involved involved in domains: domains: 11,Ile199, 11,Ile199, • 1349 quinol quinol al al

science • technique science • technique 1350 • was used. Thus, it was possible to observe the regions of i of regions the observe to possible was it Thus, used. was s MALDI-TOF purpose, this For technique. MS of tion genase of of genase X-ray crystallography. Copper (I) ion, which is probably responsible for Ar-1,2-CTD was also observed to be folded into C-terminal into folded be to observed also was Ar-1,2-CTD emty Tr6, y15 Hs1, n Hs2 respec His221 and His219, Tyr195, Tyr161, geometry, in the tr 5 with ligands connected was coordinately ey iia t te tutr o ms ctco 1,2- catechol most of structure the to similar very years. Nowadays, the studies on the enzymes widely widely enzymes the on studies the Nowadays, years. were proved to belong to the C2 symmetry group. The group. symmetry C2 the to belong to proved were analyses, conducted of result the As L69A. and A72G its derivative[2,11,12]. equipped with nitrogen laser emitting the wavelengt the emitting laser nitrogen with equipped dioxygenases Research intradiol methodsusedtodeterminestructuresof – product the releasing and structure ring the of opening in resulted Consequently, this molecule. oxygen of attack arginine- in stabilised carbanion. Arginine along with tyrosine controlled the direct resulted which C3-O, between ketonization facilitated arrangement equatorial the Tyrosinein substrate. and iron between bond peroxy of formation the was outcome process The molecule. oxygen of attack electrophilic the activating ring chelate of formation and quantitativecompositionofmixtures[14]. structures of synthesised compounds or for determining the qualitative molecular mass, structures of unknown compounds, for confirming the determining for used is technique This phase. gas the in molecules of in theregionofactivesite[8]. connector,found helical was the in presence its by enzyme stabilising simplex electron density responsible for the presence of hy of presence the for responsible density electron spholipid molecules in the helical connector of cat of connector helical the in molecules spholipid n h prn ezm. h mtns lo demonstrated also [9]. mutants 4-chlorocatechol for preference The enzyme. parent the in in larger be to out turned which complex, i substrate hollow the was differences noticeable most the of of of intrad family the as whole same the structure str site active The observed. also was phospholipid of 4 4 of catalyticconnecteddomain.wasItN-terminal with who the to which due coils random forming structure including their structures, have been a subject of of subject a been have structures, their including strain LGM S13 (Ar-1,2-CTD) and about two groups of groups two about and (Ar-1,2-CTD) S13 LGM strain f ooie. h srcue f r12CD a shown was Ar-1,2-CTD of structure The homodimer. of func a creates which part, asymmetric an in monomer (XAS) spectroscopy). (XAS) X-ray and spectroscopy (EPR) spectrometr resonance (mass paramagnetic crystallogr spectroscopy fields: and following crystallography) two to related methods rsalgah eald s o er aot h three the of about 1,2-dioxygenase catechol of learn structure to us enabled crystallography app The structure. ele ordered the displaying with molecules diffractio interaction recording radiation by uni on created X-rays a of based by is formed performance lattice method crystalline of th geometry determining and for applied been has crystallography presented be to proteins, e.g. as such molecule, ord a the allows it since biology, including science, branches many in applied is it present, At science. At first, crystallography was related to mineralogy mineralogy to related was crystallography first, At Using MALDI-TOF mass spectrometry in order to detec to order in spectrometry mass MALDI-TOF Using Mass spectrometry (MS) is the technique for analysing ionised forms h aayi o hdoyunl ,-ixgns o N of 1,2-dioxygenase hydroxyquinol of analysis The h rsac wrs n nrdo doyeae propert dioxygenase intradiol on works research The α -helices. The strongly hydrophobic space with a cle a with space hydrophobic strongly The -helices. tan E a aohr xml o apyn te ehd of method the applying of example another was 3E strain A. radioresistens A. strain LGM S13 exemplifies the applica the exemplifies S13 LGM strain Acinetobacter radioresistens Acinetobacter cis, cis cis, iol enzymes. Fe(III) Fe(III) iol enzymes. igonal bipyramidal bipyramidal igonal domaincomposed interest for a few few a for interest ered structure of of structure ered echol 1,2-dioxy echol -muconic acid or acid -muconic of industry and and industry of drophobic pho drophobic [13]. The X-ray The [13]. lication of X-ray of lication ctron clouds in in clouds ctron ucture was the the was ucture le reflected the le reflected n the enzyme- the n mutants than than mutants dioxygenases. dioxygenases. the enzymes enzymes the e dimensions dimensions e and materials materials and h of 337 nm nm 337 of h pectrometer pectrometer -dimensional -dimensional tional model model tional py (X-ray aphy its mutants: mutants: its absorption absorption t cell. The The cell. t y, electron electron y, tively. One One tively. y have one one have y arly visible visible arly ocardioides n spectra spectra n apply the the apply stronger stronger ncreased ncreased

β to be be to t pho t -sheet -sheet ies, ies, - - - -

o h autc n. aehlio itreits wer intermediates Catechol-iron one. aquatic the to the hydrophobic environment, the changes in EPR spe EPR in changes the enzym environment, the for hydrophobic the while enzyme, of solution aquatic the axial the indicated signals The site. active the to was used in the comparative research on the formati the on research comparative the in used was o h tcnqe epoe i aayig h structu the analysing in employed techniques the to two following phospholipids: glycerophosphoinositol phospholipids: following two the tested phospholipid [9]. phospholipid tested the gnal could suggest the presence of hydrophilic part hydrophilic of presence the suggest could gnal immobilised later in the hydrophobic environment [1 environment hydrophobic the in later immobilised tahet ecin n h ognc niomn i c in environment organic the in reaction attachment sl significant the It indicated gradually. occurring int was substrate the when administration the after environment the observed were on signif in Moreover, EPR the spectrum changes could depending enzyme which of hexane, conformation with lyophilisate the in w heterogeneity centre The environment. centre iron homoge the showed environment aquatic the in enzyme The than range in case of environment. the aquatic hex for signals the and observed, were resonance of Two fun state. transition important an of intermediates formation emerging of number a by resulting explained The be 3,4-dioxygenases. protocatechuate for site. active the in heterogeneity considerable and upne i hxn udr neoi cniin. The th attaching of conditions. moment the at anaerobic changing was under spectrum hexane in suspended lyophi and 8.5 pH of buffer the in suspended used enzyme were samples temperatures of types at following EPR two and helium purpose, that an For solvents organic environment. in substrate the with along 437 and 10.3x10 of catechol 1,2-dioxygenase complex of of complex 1,2-dioxygenase catechol of The spins. electron testing on based is method This Fe(III) bythesubstrate[12]. of this ion did not change during the exchange of amino acid ligands of complexes with ions of transition metals having inc having inorganic metals transition of and ions with complexes (organic electron unpaired one least using the absorption edge method, exhibited their energy – 10.8x10chlorocatechol 1,2-dioxygenase, obtained through X-ray spectroscopy and 1,2-dioxygenase hydroxyquinol for complexes enzyme-substrate of spectra The dianions. catechol as site active the to attached were phosphoinositol monophosphate. However, an attempt attempt an However, monophosphate. phosphoinositol sites of hydroxyquinol 1,2-dioxygenase of 1,2-dioxygenase hydroxyquinol of sites active the test to used was XAS object. tested X-raya of on radiation action the employs It spectrometry. absorption atomic to belonging of the observation, it was assumed that the substrates of intradiol intradiol of substrates the dioxygenases characterised that by two assumed hydroxy groups in was the it observation, basis the the On of site. active enzyme the in ion metal with substrate of significant change in the active site resulting from the direct interaction the indicated They of important. also formation were complex the enzyme-substrate during interference and signal the weaker noticeable suggested The ligands. calculations 5 with coordinated chromophore performed as Fe(III) of presence The ligands. nitrogen oxygen and with combined metal the for typical were spectra obtained The compared. were substrates with complexes their and enzymes of 1,2-dioxygenase chlorocatechol in order to determine the types of phospholipids pr phospholipids of types the determine to order in phospholipids standard the for obtained signals The lical connector of the tested enzyme. It was the ba the was It enzyme. tested the of connector lical failed due to too weak signal in the regions of hyd of regions the in signal weak too to due the in failed present was them of which unambiguously mine spholipid chains, whereas the regions characterised regions the whereas chains, spholipid X-ray absorption (XAS) spectroscopy is a widely applied technique Electron paramagnetic resonance (EPR) spectroscopy spectroscopy (EPR) resonance paramagnetic Electron -2 eV respectively. It indicated that the coordination number . erythropolis R. nr 12/2012 • 66tom N. Simplex N. . putidaP. owdown of catechol of catechol owdown bonding of iron ion ion iron of bonding tan 1CP. Native strain spectra analysis of analysis spectra sis for identifying identifying for sis of phospholipid. phospholipid. of omplete omplete were compared compared were This was typical typical was This strain 3E and of and 3E strain damental values values damental by a weaker si weaker a by ane had a wider a wider had ane esent in the he the in esent rophilic part of of part rophilic on mechanism mechanism on 5]. d the aquatic aquatic the d EPR method method EPR and glycero and strain DSM DSM strain roduced into into roduced y a different different a y free radicals, radicals, free lised enzyme enzyme lised ortho immediately immediately state could could state e present in in present e as observed observed as : lyophilised lyophilised : ctrum were were ctrum res with at at with res causing the the causing e substrate substrate e neity of the the of neity e probably probably e connector connector omparison omparison o deter to of liquid liquid of nature. nature. position tested tested d belongs belongs shell). shell). -2 eV - - - -

Literature Summary eoig h fnaetl rprto apid n bioremediation in applied processes. preparation fundamental the becoming often more and more are which enzymes degradation for engineering genetic of methods the improving for opportunity an creates way a such in acquired knowledge Consequently, the enzymes. mutant and cleavage mechanisms and distinguishing the differences between parent complex the describing for also but composition, their understanding structures of intradiol dioxygenases creates the possibility for not only 9. 9. 3. 3. 10. 10. 1. 1. 2. 2. 4. 4. 6. 6. 11. 11. 8. 8. 5. 5. 7. 7. 12. 12. 13. 13. 14. 14. 15. 15. h Fcly f iceity t h Uiest o Si of University the at Biochemistry of Faculty the involved in their decomposition. their in involved problem the in a with particu compounds of aromatic engaged biodegradation been has S she of years, University many the For at Depar the Protection at Environmental thesis and doctoral her defended she 1999, single crystal microspectrophotometry: a multidisci single microspectrophotometry: crystal Visvaganesan K., Ramachitra S., Palaniandavar M.: M.: Palaniandavar S., Ramachitra K., Visvaganesan xygenation and product selectivity product and xygenation processes A., Golovleva L., Schloemann M., Briganti F.: Briganti M., Schloemann L., Golovleva A., involved in polychlorinated aromatics biodegradatio aromatics polychlorinated in involved simpl Nocardioides from 1,2-dioxygenase droxyquinol xygenases Wojcieszyńska D., Guzik U., Greń I., Perkosz M., Hu M., Perkosz I., Greń U., Guzik D., Wojcieszyńska catechol 1,2 dioxygenase 1,2 catechol sione E., Giunta C., Rizzi M..: M..: Rizzi C., Giunta E., sione Vaillancourt F.H, J.T.,L.D: Vaillancourt Bolin Eltis Micalella C., Martignon S., Bruno S., Pioselli B., B., Pioselli S., Bruno S., Martignon C., Micalella 280 Olaniran A.O., Igbinosa E.O.: E.O.: Igbinosa A.O., Olaniran tophilia KB2 in the presence of aromatic compounds compounds of aromatic presence in the KB2 tophilia Danuta Danuta by S of mononitrophenols biotransformation Enhanced Hu M., Perkosz U., Guzik D., Wojcieszyńska I., Greń the testing for methods research modern of application The ui U, rń . Hpr-oue K, Wojcieszyńska K., Hupert-Kocurek I., Greń U., Guzik 1,2-dioxygenase from the new aromatic compounds – d – compounds aromatic new the from 1,2-dioxygenase nas putida strain N6 strain putida nas Microbiol. Biotechnol. 2010, 2010, Biotechnol. Microbiol. e-mail: [email protected]; phone:+4832 2009576 Bugg Bugg T.D.H.: Borowski T.,Borowski P.E.M.:Siegbahn Costas M., Mehn M.P., Jensen M.P., Que L.: L.: M.P., Que M.P., Jensen Mehn M., Costas city of facially coordinating tridentate phenolate phenolate tridentate city of coordinating facially A.P., I.P.: Solyanikova nol.2011, nol.2011, systems cometabolic in KB2 strain tophilia errn M, efr J, rvi V, he M, Kas M., V., Thiel Travkin J., Seifert M., Ferraroni nonuclear nonheme iron active sites: enzymes, model enzymes, sites: active iron nonheme nonuclear ses dels enzyme–substrate adducts of catechol dioxygenase enzymes dioxygenase catechol of adducts enzyme–substrate of environmental concern: properties, distribution distribution properties, concern: environmental of Chem. Rev. 2004, Rev. 2004, Chem. Induction of aromatic ring: cleavage dioxygenases i dioxygenases cleavage ring: aromatic of Induction gnetic resonance study resonance gnetic Penkala T.: Penkala and hydroxyquinol dioxygenases: ring-cleaving diol Cooper A.: A.: Cooper heme iron intradiol dioxygenases: a hybrid DFT stud DFT hybrid a dioxygenases: intradiol iron heme Sanakis Y., Mamma D., Christakopoulos P., Y., Christakopoulos D., Sanakis Stamatis Mamma xygenase from Pseudomonas putidain organic media—an organic putidain Pseudomonas from xygenase Briganti F., Mangani S., Pedocchi L., Scozzafava A. Scozzafava L., F.,Pedocchi S., Briganti Mangani 2006, . FEBS Lett. 1998, 1998, Lett. FEBS . . Tetrahedron. 2003, Tetrahedron. . 2003, , 21144–21154. , 128 WOJCIESZYŃSKA – Ph.D., is an Assistant Professor in in Professor Assistant an is Ph.D., – WOJCIESZYŃSKA . Chemosphere. 2011, 2011, Chemosphere. . . Crit. Rev. Biochem. Mol. Biol. 2006, 2006, Biol. Mol. Rev. Biochem. Crit. . 27 , 12941-12953. , Zarys krystalografii Zarys Chemia biofizyczna Chemia , 805-811. , Dioxygenase enzymes: catalytic mechanisms and chemi mechanisms catalytic enzymes: Dioxygenase nr 12/2012 • tom66 104 . Int. Biodeter. Biodegr. 2011, Biodeter.Biodegr. 2011, Int. . XAS characterization of the active sites of novel i novel of sites active the of characterization XAS 433 . Int. J. Biol. Macromol. 2003, 2003, Macromol. Biol. J. Int. . , 939-986. , . Biochim. Biophys. Acta. 2011, 2011, Acta. Biophys. Biochim. . 59 , 5862. , , 7075–7101. , 26 X-ray crystallography, mass spectrometry and spectrometry mass X-ray crystallography, Mechanism for catechol ring cleavage by non-ring cleavage for catechol Mechanism . PWN, Warszawa 1978. Warszawa PWN, . . PWN, Warszawa 2010. Warszawa PWN, . Chlorophenols and other related derivatives derivatives related other and Chlorophenols , 289-295. , 83 . Inorg. Chim. Acta 2011, 2011, Acta Chim. Inorg. . , 1297–1306. , The ins and outs of ring-cleaving dio ring-cleaving of outs and ins The . World J. Microbiol. Biotech Microbiol. J. World . ligands tunes the ligands rate of dio Dioxygen activation at mo at activation Dioxygen Crystal structure of the hy the of structure Crystal 41 and microbial degradation degradation microbial and chlorocatechol dioxygenachlorocatechol plinary characterization of characterization plinary n Stenotrophomonas mal n Stenotrophomonas Caglio R., Valetti F., Valetti R., Pes Caglio n , Golovleva L.A., Jadan Jadan L.A., Golovleva , 65 of plant origin of plant lesia in Katowice. In In Katowice. in lesia chabek S., Scozzafava Scozzafava S., chabek , 241–267. , . J. Biol. Chem. 2005, 2005, Chem. Biol. J. . lar focus on enzymes on enzymes lar focus tenotrophomonas maltenotrophomonas y Functional models for for models Functional ex 3E, a key enzyme enzyme key a 3E, ex s, and intermediates and s, 33 . J. Am. Chem. Soc. Soc. Chem. Am. J. . H.: H.: ilesia in Katowice. Katowice. in ilesia , 504-512. , egrading Pseudomo egrading tment of Biology Biology of tment , 101–106. , s related to the the to related s electron parama electron pert-Kocurek K pert-Kocurek pert-Kocurek K.: K.: pert-Kocurek Catechol 1,2-dioCatechol 1814 : the lewis basi lewis the : D.: D.: 378 , 817–823. , , 87–94. , . . World J. Catechol Catechol cal cal mo ntra .: .: ------. h Fcly f iceity t h Uiest o Si of University the at Biochemistry of Faculty the years, she has been engaged in studies on genetic r genetic on studies in engaged been has she years, degradation of arenes. of degradation ba genetic and enzymatic an on studies in engaged been Biology of Katowice Department in Silesia of University the at the Protection at thesis doctoral her Katowi in Silesia of University the at Biochemistry compound degradation. compound aehl ,-ixgns ad rtctcut 3,4-di protocatechuate and maltophilia Stenotrophomonas 1,2-dioxygenase int two catechol of description biochemical the presents she Katowi in Silesia of University the at Biochemistry of Siles University at the Protection Environmental Depar the at thesis doctoral her defended she 2000, • • Topics: • • • Targets: platform for environmental scientists with emphasis • • • • Four one-daysatelliteevents: • • • 14 e-mail: [email protected];phone:+48322009576 rzl GZK P.. i a Assat rfso in Professor Assistant an is Ph.D., – GUZIK Urszula at thesis master’s her writing is SITNIK Małgorzata P Assistant an is Ph.D., – HUPERT-KOCUREK Katarzyna e-mail: [email protected];phone:+48322009462 e-mail: [email protected];phone:+48322009576 th Water pollution and treatment – Green and sustainable industrial ol n sdmn pluin Tasomto ad ae of fate and Transformation – pollutants pollution sediment and Soil and riskassessment Atmospheric chemistry and aerosols – Modelling, management To contaminants awarenessforemerging generate fate ofchemicalsintheenvironment the to related aspects applicable and fundamental up-coming Todiscuss and existing with environmental issues research pioneering link To mining pollutionandremediation on perspectives and present Past, later: years 15 Aznalcollar Cyanobacterial toxins and occurrence Illicit drugsinwastewaters Analysis, retardants: exposure flame Alternative Emerging pollutants ecosystems (Eco-)Toxicology:and biota on Pollutantseffects and exposure chemistry CE 03 rvds uiu cmuiain n discu and communication unique a provides 2013 ICCE EuCheMSInternationalConferenceonChemistry and theEnvironment(ICCE2013) Web http://www.icce2013.org/ site: Barcelona, Spain,Europe 25 –28June2013 strain KB2. strain ce. In 2007, she defended defended she 2007, In ce. ce. In her master’s thesis, thesis, master’s her In ce. . For many years, she has has she years, many For . ia in Katowice. For many many For ia in Katowice. ses for microbiological microbiological for ses egulation of aromatic aromatic of egulation lesia in Katowice. In In Katowice. in lesia tment of Biology and and Biology of tment radiol dioxygenases: dioxygenases: radiol on chemistry. d Environmental Environmental d the Faculty of of Faculty the the Faculty of of Faculty the of of oxygenase rofessor in in rofessor • 1351 ssion

science • technique