Influence of the fusion of two subunits of the F 420 -non-reducing hydrogenase of Methanococcus voltae on its biochemical properties

Bingemann, Ruth; Pierik, Antonio J.; Klein, Albrecht

doi:10.1007/s002030000213

Cited by 2 publications

(1 citation statement)

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“…Interestingly, in Methanococcus species, the gene for the large subunit of the [NiFeSe]hydrogenase is split, and therefore the large subunit consists of two polypeptides, each contributing two ligands to the [NiFeSe]-center. A fusion of the two proteins was shown to be without effect on the kinetic and spectroscopic properties of the [NiFeSe]-hydrogenase VhuADG (78).…”

Section: Heterodisulfide Reductase-associated [Nife]-hydrogenase Mvhadgmentioning

confidence: 99%

Hydrogenases from Methanogenic Archaea, Nickel, a Novel Cofactor, and H₂ Storage

Thauer

Kaster

Goenrich

et al. 2010

Annu. Rev. Biochem.

382

401

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Most methanogenic archaea reduce CO(2) with H(2) to CH(4). For the activation of H(2), they use different [NiFe]-hydrogenases, namely energy-converting [NiFe]-hydrogenases, heterodisulfide reductase-associated [NiFe]-hydrogenase or methanophenazine-reducing [NiFe]-hydrogenase, and F(420)-reducing [NiFe]-hydrogenase. The energy-converting [NiFe]-hydrogenases are phylogenetically related to complex I of the respiratory chain. Under conditions of nickel limitation, some methanogens synthesize a nickel-independent [Fe]-hydrogenase (instead of F(420)-reducing [NiFe]-hydrogenase) and by that reduce their nickel requirement. The [Fe]-hydrogenase harbors a unique iron-guanylylpyridinol cofactor (FeGP cofactor), in which a low-spin iron is ligated by two CO, one C(O)CH(2)-, one S-CH(2)-, and a sp(2)-hybridized pyridinol nitrogen. Ligation of the iron is thus similar to that of the low-spin iron in the binuclear active-site metal center of [NiFe]- and [FeFe]-hydrogenases. Putative genes for the synthesis of the FeGP cofactor have been identified. The formation of methane from 4 H(2) and CO(2) catalyzed by methanogenic archaea is being discussed as an efficient means to store H(2).

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Section: Heterodisulfide Reductase-associated [Nife]-hydrogenase Mvhadgmentioning

confidence: 99%

Hydrogenases from Methanogenic Archaea, Nickel, a Novel Cofactor, and H₂ Storage

Thauer

Kaster

Goenrich

et al. 2010

Annu. Rev. Biochem.

382

401

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Small Proteins in Archaea, a Mainly Unexplored World

et al. 2022

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In recent years, increasing numbers of small proteins have moved into the focus of science. Small proteins have been identified and characterized in all three domains of life, but the majority remains functionally uncharacterized, lack secondary structure, and exhibit limited evolutionary conservation. While quite a few have already been described for bacteria and eukaryotic organisms, the amount of known and functionally analyzed archaeal small proteins is still very limited. In this review we compile the current state of research, show strategies for systematic approaches for global identification of small archaeal proteins and address selected functionally characterized examples. Besides, we document exemplarily for one archaeon the tool development and optimization to identify small proteins using genome wide approaches.

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Influence of the fusion of two subunits of the F 420 -non-reducing hydrogenase of Methanococcus voltae on its biochemical properties

Cited by 2 publications

References 11 publications

Hydrogenases from Methanogenic Archaea, Nickel, a Novel Cofactor, and H₂ Storage

Hydrogenases from Methanogenic Archaea, Nickel, a Novel Cofactor, and H₂ Storage

Small Proteins in Archaea, a Mainly Unexplored World

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Influence of the fusion of two subunits of the F 420 -non-reducing hydrogenase of Methanococcus voltae on its biochemical properties

Cited by 2 publications

References 11 publications

Hydrogenases from Methanogenic Archaea, Nickel, a Novel Cofactor, and H2 Storage

Hydrogenases from Methanogenic Archaea, Nickel, a Novel Cofactor, and H2 Storage

Small Proteins in Archaea, a Mainly Unexplored World

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Product

Resources

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Hydrogenases from Methanogenic Archaea, Nickel, a Novel Cofactor, and H₂ Storage

Hydrogenases from Methanogenic Archaea, Nickel, a Novel Cofactor, and H₂ Storage