Nickel hydrogenases: in search of the active site

Albracht, S.P.J.

doi:10.1016/0005-2728(94)90036-1

Cited by 470 publications

(501 citation statements)

References 207 publications

(382 reference statements)

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“…This is in agreement with an earlier proposal based on spectroscopic data (Surerus et al, 1994;Albracht, 1994), indicating the presence of a lone low-spin Fe(II1) ion close to the nickel. The structure also shows that four conservative Cys residues from the large subunit are involved in binding the two metal ions in the active site, while all of the Fe-S clusters are coordinated by the small subunit, confirming earlier proposals (Voordouw, 1992;Albracht, 1994). Interestingly, the crystal structure indicates the presence of three non-protein groups as ligands for one of the metal ions in the active site.…”

Section: Added In Proofsupporting

confidence: 93%

“…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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confidence: 99%

“…These sequences have been compared and discussed in some recent publications (Przybyla et al, 1992;Voordouw, 1992;Wu & Mandrand, 1993;Albracht, 1993Albracht, , 1994. All enzymes contain a conserved amino acid sequence motif DPCxxCxxH at the carboxy terminus of the large subunit.…”

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confidence: 99%

“…The small subunits of 17 nickel hydrogenases each contain 10 conserved Cys residues (Voordouw, 1992;Wu & Mandrand, 1993;Albracht, 1993) and were termed standard nickel hydrogenases (Albracht, 1994). The well-studied enzyme from Desulfovibrio gigas (Fernandez et al, 1986;Teixeira et al, 1989) belongs to this category.…”

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confidence: 99%

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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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Section: Added In Proofsupporting

confidence: 93%

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confidence: 99%

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confidence: 99%

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confidence: 99%

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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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“…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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Ab initio investigation of the structural and electronic differences between active-site models of [NiFe] and [NiFeSe] hydrogenases

Gioia¹,

Fantucci²,

Guigliarelli

et al. 1999

Int. J. Quant. Chem.

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ABSTRACT:The structural and electronic differences between coordination w x w x compounds which model NiFe and NiFeSe hydrogenase active sites were investigated using quantum chemical methods. A previous study showed that the structural and electronic properties of these model compounds are largely consistent with available w x Ž experimental data in the case of NiFe hydrogenases L. De Gioia, P. Fantucci, .

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Nickel hydrogenases: in search of the active site

Cited by 470 publications

References 207 publications

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

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

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

Ab initio investigation of the structural and electronic differences between active-site models of [NiFe] and [NiFeSe] hydrogenases

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