Evidence for the Periplasmic Location of Hydrogenase in
            <i>Desulfovibrio gigas</i>

Bell, George R.; LeGall, Jean; Peck, Harry D.

doi:10.1128/jb.120.2.994-997.1974

Cited by 97 publications

(25 citation statements)

References 19 publications

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“…The periplasmic localization of D. gigas hydrogenase has also been used to simplify the purification procedure by reducing the amount of proteins in the crude extract. This was achieved by simply 'washing' the cells with a slightly alkaline buffer [23,154]. A better purification procedure used seven chromatographic steps and led to an enzyme which had a specific activity (expressed in micromoles H 2 produced per minute per mg protein) of 90.8 in the hydrogen evolution assay [155,156].…”

Section: Localization Purification and Molecular Compositionmentioning

confidence: 99%

“…The large subunit protein also lacks an obvious internal, hydrophobic signal-like sequence found in the [Fe] hydrogenase. As the D. gigas enzyme is localized in the periplasmic space of the cell [154], it once again appears that a mechanism must exist to co-translocate both hydrogenase subunits through the cytoplasmic membrane by means of the leader sequence present on the small subunit [82].…”

Section: Molecular Biologymentioning

confidence: 99%

“…D. vulgaris (Hildenborough) is the only species found to contain all three hydrogenase genes and this has been confirmed by enzymological studies. D. gigas ap- Table 7 The cellular localization of the three classes of hydrogenases from Desulfovtbrio pears to contain only one gene for a [NiFe] hydrogenase, and this enzyme has been isolated from the periplasm [154]. A periplasmic localization of hydrogenase may not necessarily preclude energy recovery by hydrogenase or even H 2 cycling.…”

Section: Hy-drogenasesmentioning

confidence: 99%

“…This curious distribution of the hydrogenases raises important questions regarding the evolutionary relationships within Desulfovibrio, the enzymatic and bioenergetic functions of the different hydrogenases, the mechanisms involved in their different cellular localizations, and the attachment to the membranes. Additionally, the relationship among the three types of hydrogenases and the periplasmic tetraheme cytochrome c 3 [23,108,154,[221][222][223], which could serve as a cofactor for each of the hydrogenases, needs to be reinvestigated with regard to specificity and cellular localization. Using membrane-inlet mass spectrometry, D. vulgaris (Hildenborough) has been shown to carry out hydrogen cycling during the oxidation of pyruvate with sulfate [224] and the proposed mechanism is shown in Fig.…”

Section: Hy-drogenasesmentioning

confidence: 99%

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The three classes of hydrogenases from sulfate-reducing bacteria of the genus Desulfovibrio

Fauque

1988

FEMS Microbiology Letters

104

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SUMMARYThree types of hydrogenases have been isolated from the sulfate-reducing bacteria of the genus Desulfovibrio. They differ in their subunit and metal compositions, physico-chemical characteristics, amino acid sequences, immunological reactivities, gene structures and their catalytic properties. Broadly, the hydrogenases can be considered as 'iron only' hydrogenases and nickel-containing hydrogenases. The iron-sulfur-containing hydrogenase ([Fe] hydrogenase) contains two ferredoxin-type (4Fe-4S) clusters and an atypical ironsulfur center believed to be involved in the activation of H E. 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 sensi-Correspondence to: G. Fauque, Section Enzymologie et Biochimie Bact6rienne, ARBS, CEN Cadarache, 13108 Saint-Paul-Lez-Durance Cedex, France. tive to CO and NO 2. 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-xS) 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 NO 2 . 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 0168-6445/88/$03.50

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Section: Localization Purification and Molecular Compositionmentioning

confidence: 99%

Section: Molecular Biologymentioning

confidence: 99%

Section: Hy-drogenasesmentioning

confidence: 99%

Section: Hy-drogenasesmentioning

confidence: 99%

See 2 more Smart Citations

The three classes of hydrogenases from sulfate-reducing bacteria of the genus Desulfovibrio

Fauque

1988

FEMS Microbiology Letters

104

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“…19 Desulfovibrio hydrogenases are found to catalyze both hydrogen production and uptake with low potential multiheme cytochromes, such as cytochromes c 3 , acting as donors or acceptors. 20 Several types of soluble polyheme cytochromes c have been isolated and characterized in the anaerobic sulphate-reducing bacteria belonging to the Desulfovibrio genus. Among them are the tetraheme cytochrome c 3 (Mr 13,000), 21 the octaheme cytochrome c 3 (Mr 26,000), 22 and the hexadecaheme cytochrome Hmc.…”

Section: Introductionmentioning

confidence: 99%

Kinetics and interaction studies between cytochrome c3 and Fe‐only hydrogenase from Desulfovibrio vulgaris hildenborough

Brugna¹,

Giudici-Orticoni²,

Spinelli³

et al. 1998

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Hydrogenases from Desulfovibrio are found to catalyze hydrogen uptake with low potential multiheme cytochromes, such as cytochrome c3, acting as acceptors. The production of Fe-only hydrogenase from Desulfovibrio vulgaris Hildenborough was improved with respect to the growth phase and media to determine the best large-scale bacteria growth conditions. The interaction and electron transfer from Fe-only hydrogenase to multiheme cytochrome has been studied in detail by both BLAcore and steady-state measurements. The electron transfer between [Fe] hydrogenase and cytochrome c3 appears to be a cooperative phenomenon (h = 1.37). This behavior could be related to the conductivity properties of multihemic cytochromes. An apparent dissociation constant was determined (2 x 10(-7) M). The importance of the cooperativity for contrasting models proposed to describe the functional role of the hydrogenase/cytochrome c3 complex is discussed. Presently, the only determined structure is from [NiFe] hydrogenase and there are no obvious similarities between [NiFe] and [Fe] hydrogenase. Furthermore, no crystallographic data are available concerning [Fe] hydrogenase. The first results on crystallization and X-ray crystallography are reported.

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Kinetics and interaction studies between cytochrome c3 and Fe-only hydrogenase fromDesulfovibrio vulgaris hildenborough

et al. 1998

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Evidence for the Periplasmic Location of Hydrogenase in Desulfovibrio gigas

Abstract: Hydrogenase has been found to be located in the periplasmic space of Desulfovibrio gigas , and it is proposed that hydrogenase plays an important and specific role in interspecies hydrogen transfer.

Cited by 97 publications

References 19 publications

The three classes of hydrogenases from sulfate-reducing bacteria of the genus Desulfovibrio

The three classes of hydrogenases from sulfate-reducing bacteria of the genus Desulfovibrio

Kinetics and interaction studies between cytochrome c3 and Fe‐only hydrogenase from Desulfovibrio vulgaris hildenborough

Kinetics and interaction studies between cytochrome c3 and Fe-only hydrogenase fromDesulfovibrio vulgaris hildenborough

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