The structure and mechanism of iron-hydrogenases

Adams, Michael W. W.

doi:10.1016/0005-2728(90)90044-5

Cited by 754 publications

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“…Hydrogen metabolism in microorganisms is mediated by metallo-enzymes called hydrogenases [1,2]. These enzymes can catalyze both hydrogen oxidation, which furnishes the cell with low-potential electrons, and proton reduction, that re-oxidizes electron carriers involved in fermentation or photosynthesis, according to the reaction: H 2 , 2H + + 2e À .…”

Section: Introductionmentioning

confidence: 99%

The role of the maturase HydG in [FeFe]‐hydrogenase active site synthesis and assembly

et al. 2009

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a b s t r a c t[FeFe]-hydrogenases catalyze the protons/hydrogen interconversion through a unique di-iron active site consisting of three CO and two CN ligands, and a non-protein SCH 2 XCH 2 S (X = N or O) dithiolate bridge. Site assembly requires two ''Radical-S-adenosylmethionine (SAM or AdoMet)" iron-sulfur enzymes, HydE and HydG, and one GTPase, HydF. The sequence homology between HydG and ThiH, a Radical-SAM enzyme which cleaves tyrosine into p-cresol and dehydroglycine, and the finding of a similar cleavage reaction catalyzed by HydG suggests a mechanism for hydrogenase maturation. Here we propose that HydG is specifically involved in the synthesis of the dithiolate ligand, with two tyrosine-derived dehydroglycines as precursors along with an [FeS] cluster of HydG functioning both as electron shuttle and source of the sulfur atoms.

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Section: Introductionmentioning

confidence: 99%

The role of the maturase HydG in [FeFe]‐hydrogenase active site synthesis and assembly

et al. 2009

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“…Recently, a H2-forming enzyme was described, in which no metals could be detected at all: methylenetetrahydromethanopterin dehydrogenase from Methanobacterium thermoautotrophicum (Zirngibl et al, 1992). Different aspects of hydrogenases have been reviewed over the past 6 years (Fauque et al, 1988;Adams, 1990;Albracht, 1990Albracht, , 1994Przybyla et al, 1992;Voordouw, 1992;Wu & Mandrand, 1993).…”

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Infrared-Detectable Group Senses Changes in Charge Density on the Nickel Center in Hydrogenase from Chromatium vinosum

Bagley

Duin²,

Roseboom³

et al. 1995

Biochemistry

218

217

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An infrared-detectable group senses changes in charge density on the nickel center in hydrogenase from Chromatium vinosum Bagley, K.A.; Duin, E.L.; Roseboom, W.; Albracht, S.P.J.; Woodruff, W.H. General rights It is not permitted to download or to forward/distribute the text or part of it without the consent of the author(s) and/or copyright holder(s), other than for strictly personal, individual use, unless the work is under an open content license (like Creative Commons). Disclaimer/Complaints regulationsIf you believe that digital publication of certain material infringes any of your rights or (privacy) interests, please let the Library know, stating your reasons. In case of a legitimate complaint, the Library will make the material inaccessible and/or remove it from the website. Please Ask the Library: http://uba.uva.nl/en/contact, or a letter to: Library of the University of Amsterdam, Secretariat, Singel 425, 1012 WP Amsterdam, The Netherlands. You will be contacted as soon as possible. ABSTRACT: Fourier transform infrared studies of nickel hydrogenase from Chromatium vinosum reveal the presence of a set of three absorption bands in the 2100-1900 cm-1 spectral region. These bands, which do not arise from carbon monoxide, have line widths and intensities rivaling those of a band arising from the carbon monoxide stretching frequency (v(C0)) in the Ni(I1)CO species of this enzyme

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“…Biochemical studies have clearly established the existence of two main groups of enzymes in sulfate-reducing bacteria of the genus Desulfovibrio, the one containing either nickel or nickel and selenium atoms in addition to iron/sulfur clusters ([NiFeI-hydrogenases and [NiFeSeI-hydrogenases) and the other containing exclusively iron-sulfur clusters ([Felhydrogenases). These hydrogenases differ in their metal-centre composition, mechanistic properties, sensitivity to inhibitors, amino acid sequences and immunological properties [ 11.In contrast to the widespread nickel-containing hydrogenases, the known [Fel-hydrogenases, which exhibit high catalytic activity, form a small family of proteins [2]. Among these enzymes, the periplasmic [Fel-hydrogenase from Desulfovibrio vulgaris Hildenborough has been thoroughly investigated by a variety of biochemical and spectroscopic techniques [3 -111.…”

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confidence: 99%

“…In contrast to the widespread nickel-containing hydrogenases, the known [Fel-hydrogenases, which exhibit high catalytic activity, form a small family of proteins [2]. Among these enzymes, the periplasmic [Fel-hydrogenase from Desulfovibrio vulgaris Hildenborough has been thoroughly investigated by a variety of biochemical and spectroscopic techniques [3 -111.…”

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Further characterization of the [Fe]‐hydrogenase from Desulfovibrio desulfuricans ATCC 7757

Hatchikian

Forget

Fernández

et al. 1992

European Journal of Biochemistry

146

148

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The properties of the periplasmic hydrogenase from Desulfovibrio desulfuricans ATCC 7757, previously reported to be a single-subunit protein [Glick, B. R., Martin, W. G. and Martin, S. M. (1980) Can. J. Microbiol. 26,1214-12231 were reinvestigated. The pure enzyme exhibited a molecular mass of 53.5 kDa as measured by analytical ultracentrifugation and was found to comprise two different subunits of 42.5 kDa and 11 kDa, with serine and alanine as N-terminal residues, respectively. The N-terminal amino acid sequences of its large and small subunits, determined up to 25 residues, were identical to those of the Desulfnvibrio vulgaris Hildenborough [Fel-hydrogenase. D. desulfuricans ATCC 7757 hydrogenase was free of nickel and contained 14.0 atoms of iron and 14.4 atoms of acidlabile sulfur/molecule and had ~4 0 0 , 52.5 mM-l . cm-l. The purified hydrogenase showed a specific activity of 62 kU/mg of protein in the H2-uptake assay, and the H2-uptake activity was higher than H2-evolution activity. The enzyme isolated under aerobic conditions required incubation under reducing conditions to express its maximum activity both in the H,-uptake and 2H2/'H2 exchange reaction. The ratio of the activity of activated to as-isolated hydrogenase was approximately 3. EPR studies allowed the identification of two ferredoxin-type [4Fe-4SI1+ clusters in hydrogenase samples reduced by hydrogen. In addition, an atypical cluster exhibiting a rhombic signal (g values 2.10, 2.038, 1.994) assigned to the H,-activating site in other [Fel-hydrogenases was detected in partially reduced samples. Molecular properties, EPR spectroscopy, catalytic activities with different substrates and sensitivity to hydrogenase inhibitors indicated that D. desulfuricans ATCC 7757 periplasmic hydrogenase is a [Fel-hydrogenase, similar in most respects to the well characterized [Fel-hydrogenase from D. vulgaris Hildenborough.Hydrogenase, an enzyme widely distributed among microorganisms, catalyzes the reversible oxidation of molecular hydrogen. Biochemical studies have clearly established the existence of two main groups of enzymes in sulfate-reducing bacteria of the genus Desulfovibrio, the one containing either nickel or nickel and selenium atoms in addition to iron/sulfur clusters ([NiFeI-hydrogenases and [NiFeSeI-hydrogenases) and the other containing exclusively iron-sulfur clusters ([Felhydrogenases). These hydrogenases differ in their metal-centre composition, mechanistic properties, sensitivity to inhibitors, amino acid sequences and immunological properties [ 11.In contrast to the widespread nickel-containing hydrogenases, the known [Fel-hydrogenases, which exhibit high catalytic activity, form a small family of proteins [2]. Among these enzymes, the periplasmic [Fel-hydrogenase from Desulfovibrio vulgaris Hildenborough has been thoroughly investigated by a variety of biochemical and spectroscopic techniques [3 -111. The protein exhibits a molecular mass of 56 kDa and is composed of two different subunits (46 kDa and 10 kDa).Correspondence to E. C . ...

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The structure and mechanism of iron-hydrogenases

Cited by 754 publications

References 179 publications

The role of the maturase HydG in [FeFe]‐hydrogenase active site synthesis and assembly

The role of the maturase HydG in [FeFe]‐hydrogenase active site synthesis and assembly

Infrared-Detectable Group Senses Changes in Charge Density on the Nickel Center in Hydrogenase from Chromatium vinosum

Further characterization of the [Fe]‐hydrogenase from Desulfovibrio desulfuricans ATCC 7757

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