The three classes of hydrogenases from sulfate-reducing bacteria of the genus Desulfovibrio (original) (raw)

Journal Article

1Section Enzymologie et Biochimie Bactérienne, ARBS, CEN Cadarache, 13108 Saint-Paul-Lez-Durance Cedex, France

Corrrespondence to: G. Fauque, Section Enzymologie et Biochimie Bactérienne, ARBS, CEN Cadarache, 13108 Saint-Paul-Lez-Durance Cedex, France.

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2School of Chemical Sciences, Department of Biochemistry, University of Georgia, Athens, GA 30602, U.S.A.

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3Centro de Quimica Estrutural, Universidade Nova de Lisboa, Complexo I, IST, Av. Rovisco Pais, 1096 Lisboa Cedex, Portugal

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4Department of Physics, Emory University, Atlanta, GA 30322, U.S.A.

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1Section Enzymologie et Biochimie Bactérienne, ARBS, CEN Cadarache, 13108 Saint-Paul-Lez-Durance Cedex, France

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2School of Chemical Sciences, Department of Biochemistry, University of Georgia, Athens, GA 30602, U.S.A.

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3Centro de Quimica Estrutural, Universidade Nova de Lisboa, Complexo I, IST, Av. Rovisco Pais, 1096 Lisboa Cedex, Portugal

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2School of Chemical Sciences, Department of Biochemistry, University of Georgia, Athens, GA 30602, U.S.A.

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1Section Enzymologie et Biochimie Bactérienne, ARBS, CEN Cadarache, 13108 Saint-Paul-Lez-Durance Cedex, France

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3Centro de Quimica Estrutural, Universidade Nova de Lisboa, Complexo I, IST, Av. Rovisco Pais, 1096 Lisboa Cedex, Portugal

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Accepted:

02 November 1988

Published:

01 December 1988

Cite

G. Fauque, H.D. Peck, J.J.G. Moura, B.H. Huynh, Y. Berlier, D.V. DerVartanian, M. Teixeira, A.E. Przybyla, P.A. Lespinat, I. Moura, J. LeGall, The three classes of hydrogenases from sulfate-reducing bacteria of the genus Desulfovibrio, FEMS Microbiology Reviews, Volume 4, Issue 4, December 1988, Pages 299–344, https://doi.org/10.1111/j.1574-6968.1988.tb02748.x
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Abstract

Three types of hydrogenases have been isolated from the sulfate-reducing bacteria of the genus Desulfobibrio. They differ in their subunit and metal compositions, physico-chemical characteristics, amino acid sequences, immunological ractivities, gene structures and their catalytic properties. Broadly, the hydrogenases can be considered as ‘iron only’ hydrogenases and nickel-containing hydrogenases. The iron-sulfur-containg hydrogenase ([Fe] hydrogenase) contains two ferredoxin-type (4Fe-4S) clusters and an atypical iron-sulfur center belived to be involved in the activation of H2. The [Fe] hydrogenase has the highest specific activity in the evolution and consumption of hydrogen and in the proton-deuterium exchange reaction and this enzyme is the most sensitive to CO and NO2−. It is not present in all species of Desulfovibrio.

The nickel-(iron-sulfur)-containing hydrogenases ([NiFe] hydrogenases) possess two (4Fe-4S) centers and one (3Fe-_x_S) cluster in addition to nickel and have been found in all species of Desulfovibrio so far investigated. The redox active nickel is ligated by at least two cysteinyl thiolate residues and the [NiFe] hydrogenases are particularly resistant to inhibitors such as CO and NO2−. The genes encoding the large and small subunits of a periplasmic and a membrane-bound species of the [NiFe] hydrogenase have been cloned in Escherichia (E.) coli and sequenced. Their derived amino acid sequences exhibit a high degree of homology (70%); however, they show no obvious metal-binding sites or homology with the derived amino acid sequence of the [Fe] hydrogenase. The third class is represented by the nickel-(ironsulfur)-selenium-containing hydrogenases ([NiFe-Se] hydrogenases) which contain nickel and selenium in equimolecular amounts plus (4Fe-4S) centers and are only found in some species of Desulfovibrio. The genes encoding the large and small subunits of the periplasmic hydrogenase from Desulfovibrio (D.) baculatus (DSM 1743) (for abbreviations see appendix) have been cloned in E. coli and sequenced. The derived amino acid sequence exhibits homology (40%) with the sequence of the [NiFe] hydrogenase and the carboxy-terminus of the gene for the large subunit contains a codon (TGA) for selenocysteine in a position homologous to a codon (TGC) for cysteine in the large subunit of the [NiFe] hydrogenase. EXAFS and EPR studies with the 77Se-enriched D. baculatus hydrogenase indicate that selenium is a ligand to nickel and suggest that the redox active nickel is ligated by at least two cysteinyl thiolate and one selenocysteine selenolate residues. The data suggest that the chemical behavior of the active site nickel is modified by the presence of selenium such that the [NiFeSe] hydrogenase exhibits an H2/HD ratio greater than one in the proton-deuterium exchange reaction and possesses a specific sensitivity to CO and NO2− inhibition, intermediate between that of the [Fe] and [NiFe] hydrogenases.

All of the genes for the small subunits of the three types of hydrogenases code for signal peptides; however, the genes for the large subunits do not appear to code for signal peptides and the mechanism involved in the translocation of the large subunits is of major concern. Studies on the functional role of the three Desulfovibrio hydrogenases are still in their infancy but it appears that multiple hydrogenase activities result from the need to independently regulate various redox couples such as the H2/fumarate and formate/hydrogenlyase couples in E. coli. Alternatively, the three types of hydrogenases have been identified and localized in D. vulgaris (Hildenborough) and appear to be involved in hydrogen cycling and the generation of a proton gradient.

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