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Marine Haloperoxidases

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Marine Haloperoxidases chem. Rev. 1998, 93, 1937-1944 Marine Haloperoxidases Alison Butler’ and J. V. Walker oepemnmt of ~%~II/SIIY. (~vasllyof cawom$. anta &&am. CaBlanh, 93106 Reodved A@ 20, 1993 (Revlsed Manusmt Racslved May 20, 1993) Contents I. Introduction 1937 A. Halogenated Compounds in the Marine 1937 Envlronment p: ? E. Marine Habperoxidases 1938 6 1. Types of Marine Haioperoxidases 1938 8. 2. Standard Assay of Habperoxidase 1939 Activity 11. Vanadium Bromoperoxidase 1939 A. Characterlstics of V-ErPO 1939 1. Isoiatlon and Purlflcation of VgrpO 1939 2. The Vanadium Sne 1939 .... .. ...:.;.. .. E. Reactivity Of V-ErpO 1940 . :. .. :. [.. 1. Halogenation and HalldeAssisted 1940 AII~~utler received her &A. from Reed College in 1977 and her Disproportionation of Hydrogen P~.D.from the University of California. San Diego. in 1962. Alter Peroxide pwMoaaal stays at UC Los Angeles and Caitech. she joked the 2. Specific Activltles 1941 faculty at UC Santa Barbara in 1986. She is a recent reciplent of an American Cancer Society. Junior Faculty Research Award, 1941 3. Enzyme Kinetics an Alfred P. Sbn Foundatlon Fellowship, and the UCSE PIOUS 4. Peroxide Selectivity 1941 TeacherlSchoiar Award. Her research interestsarein bioinaganic 5. Mechanistic Considerations 1941 chemistry and metalloblochemistry. including that of the marlne environment. C. Stability of V-ErPO 1942 D. Comment on the Putative Non-i-bma Iron 1942 Eromoperoxidases 111. Fell“ Bromoperoxidase 1942 A. Characteristics of FeHeme 1942 Eromoperoxbse E. Reactivity of FeHeme Bromoperoxidase 1942 1. Biosynthetic Investigations 1943 2. Other FeHema Haloperoxidases 1943 1V. Future Directions 1944 I. Introductlon A. Halogenated Compounds in the Msrlne Environment Jenylalne Vanessa Walker was born in St. John’s. Antigua, West Indles.in 1967. Shereceived her6.S. in ChemisbyfromCalifmia Ocean water is approximately 0.5 M in chloride, 1 State University, Bakersfield. in 1989. She is currently working on mM in bromide, and 1 pM in iodide. Given the high her Ph.D. at the University of California. Santa Barbara, under tlm halogen content, it is not surprising that marine dlrectlon of Prof. Alison Butler. Ourlng her time at UCSB she has received a University Regents Fellowship, a UCSE Graduate organisms have developed means to incorporate halo- Opportunity Fellowship. and a UCSB Graduate Reaearch Mentwship gens into their metabolites. Many of these halogenated Fellowship. Her general research interests include biolnorganic compounds are thought to be involved in chemical chemistry, natural products chemistry, and marine biochemistry. defense roles to keep predators away from a particular organism. Inmany cases these compounds are also of volatile halohydrocarbons produced in very large pharmacological interest due to their biological activ- quantities, such as bromoform, dibromomethane, meth- ities, which include antifungal, antibacterial, antine- yl iodide, bromo- and chloroanisoles, etc.14 Others oplastic, antiviral (e.g., anti-HIV), antiinflammatory, include phenolic derivatives in which the biosynthesis and other activities. of these compounds can be readily envisaged, as in The halogenatedmarine natural products encompass aeroplysinin-1 (see 1 in Figure I), an antimicrobial a very wide range of compounds. Some are simple metabolite from sponges? or 14-debromoprearaplysillin (2) from the marine sponge Druinella purpurea? both To whom mrrespondencs should be addread. of which could originate from tyrosine (see below), or 0009-2665/93/0793-1937$12.00/0 0 I993 American Chemical SocW 1938 Chemical Reviews, 1993, Vol. 93, NO. 5 Butler and Walker OMe Br Br bromoperoxidase catalyzes the oxidation of bromide and iodide by hydrogen peroxide, while iodoperoxidase catalyzes the oxidation of only iodide by hydrogen peroxide. A better system of nomenclature would be based on the enzyme’s physiological role, although at this point, that is hard to define given that the 1 concentrations of halides, hydrogen peroxide, and nature of the endogenous organic substrate are not known in many marine organisms. 1. Types of Marine Haloperoxidases Haloperoxidases have been isolated from all classes of marine algae and many other marine organisms (Table I); in addition haloperoxidase activity has been detected in many other species of algae13 and in other marine organisms. Two types of marine haloperoxi- 6 dases have been identified: (1) vanadium bromoper- 5 oxidase (V-BrPO),a non-heme enzyme, and (2) FeHeme Figure 1. Examples of marine natural products with bromoperoxidase (FeHeme-BrPO). In some cases, a important biological activities. marine haloperoxidase has been isolated, but the vanadium or FeHeme content has not been determined, the antimicrobial compound 2-(2’-bromophenoxy)- as in the marine snail Murex truncuZus.30 In addition 3,4,5,6-tetrabromophenol(3)from the sponge Dysidea.’ to these enzymes, other terrestrial haloperoxidases are Numerous chiral chlorinated and brominated terpen- known, including the first discovered haloperoxidase, oids have also been isolated, including solenolide E (4), chloroperoxidase, the FeHeme enzyme from the fungus a diterpene which is an antiinflammatory and antiviral Caldaromyces f~mago,~~mammalian haloperoxidases compound isolated from a gorgonian.8 One of the more such as eosinophil peroxidase32 and myeloper~xidase~~ famous brominated marine natural products is tyrian found in human white blood cells, salivary and lac- purple (5), isolated from a marine mollusk. Other toperoxidase found in saliva and tearsF2 and bacterial brominated and chlorinated indoles, e.g., 5-bromo-NJV- haloperoxidases (bromoperoxidase from Streptomy- dimethyltryptamine (6), from a marine ~ponge,~are ces33 and chloroperoxidase from Pseudom0nads3~)for also known. A comprehensive summary of halogenated which the identity of the active-metal species, if any, compounds is contained in a series of reviews of marine has not been determined. Recently a new enzyme, natural products by Faulkner.lo methyl transferase, was isolated from marine alga Marine natural products chemists have long invoked (Endocladia muricata) that catalyzes the formation of the role of haloperoxidases in the biogenesis of the methyl chloride.35 Methyltransferase uses S-adenosyl- halogenated marine natural products. Bromoperoxi- methionine as the carbon source. dase and iodoperoxidase activity have been well doc- umented in marine algae since the turn of the centu- Table I. Sources of Marine Haloperoxidases ry,l1J2 Haloperoxidases have been found in virtually ref(s) all classes of marine organisms. Early on, Hewson and ~~ Hager established that many species of marine algae vanadium bromoperoxidase have bromoperoxidase activity in aqueous algal ex- I. Rhodophyta (red algae) Corallina officinalis 14 tract~.~~Rhodophyta were the richest in both bro- Corallina pilulifera 15,16 moperoxidase activity and lipid halogen content; Pheo- Corallina uancouveriensis 17 phyta were the poorest. Marine haloperoxidases have Ceramium rubrum 18 now been isolated and purified to homogeneity; thus 11. Phaeophyta (brown algae) the scope of this review article will be the reactivity Alaria esculenta 19 Ascophyllum nodosum 20 and characterization of the marine haloperoxidases. Chorda filum 21 Fucus distichus 22 Laminaria digitata 23 B. Marlne Haloperoxldases Laminaria sacchirina 21 Macrocystis pyrifera 22 Haloperoxidases are enzymes that catalyze the ox- 111. Chlorophyta (green algae) idation of a halide (i.e., chloride, bromide, or iodide) by Halimeda sp. 24 hydrogen peroxide, a process which results in the FeHeme bromoperoxidases concomitant halogenation of organic substrates. I. Rhodophyta Cystoclonium purpureum 25 Rhodomela larix 26 Org-H + X- + H20, + H+ - X-Org + 2H20 11. Chlorophyta Penicillus capitatus 21,28 Penicillus lamourouxii 28 The nomenclature for the haloperoxidases has tra- Rhipocephalus phoenix 28 ditionally been based on the most electronegative halide 111. Marine worm which is able to be oxidized by HzO2 catalyzed by the Notomastus lobatus 29 enzyme. Thus chloroperoxidasecatalyzes the oxidation Ptychodera flavin laysanica 26 of chloride, bromide, and iodide by hydrogen peroxide; Thelepus setosus 26 Marine Haloperoxidases Chemical Reviews, 1993, Vol. 93, No. 5 1090 be achieved by addition of excess vanadate and sub- sequent removal of adventitiously bound vanadium(V) by dialysi~.~~?~~~~~While the physical characteristics of V-BrPO isolated from marine algae are all very similar, some differences in reactivity have been observed, such Figure 2. Halogenation of monochlorodimedone (MCD) as specific activity (see below). V-BrPO (Ascophyllum catalyzed by haloperoxidases. nodosum) has been crystallized, although refined structural data have not been reported yet.39 The 2. Standard Assay for Haloperoxidase Activity crystals defract to 2.4-A resolution. Four molecules are The standard assay for haloperoxidase activity is the present per asymmetric subunit. halogenation of monochlorodimedone (MCD; 2-chloro- Isozymes of vanadium bromoperoxidases from A. 1,&dimedone) using hydrogen peroxide as the oxidant nodosum have been isolated which differ in carbohy- of the halide (Figure 2).31 drate ~ontent.'~~~~The more abundant bromoperoxi- The halogenation of MCD is followed spectropho- dase based on isolated yield, V-BrPO-I, was found in tometrically at 290 nm, which monitors the loss of MCD the thallus and the other bromoperoxidase, V-BrPO- in the enolform (t = 20 000M-l cm-l). Bromoperoxidase 11, was reported to be present on the thallus surface.37 activity
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