Nickel-dependent hydrogenase

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Nickel-dependent hydrogenase
Identifiers
SymbolNiFeSe_Hases
PfamPF00374
InterProIPR001501
PROSITEPDOC00400
SCOP21frv / SCOPe / SUPFAM
TCDB3.D.7
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
PDB1e3dD:50-543 1h2rL:59-552 1ubjL:59-552

1ublL:59-552 1wulL:59-552 1h2aL:59-552 1ubtL:59-552 1wujL:59-552 1ubuL:59-552 1ubkL:59-552 1ubhL:59-552 1ubmL:59-552 1wukL:59-552 1wuhL:59-552 1wuiL:59-552 1uboL:59-552 1ubrL:59-552 1frfL:50-549

1yqwQ:50-548 1yq9H:43-535 1cc1L:49-498

Hydrogenases are enzymes that catalyze the reversible activation of hydrogen and which occur widely in prokaryotes as well as in some eukaryotes. There are various types of hydrogenases, but all of them seem to contain at least one iron-sulphur cluster. They can be broadly divided into two groups: hydrogenases containing nickel and, in some cases, also selenium (the [NiFe] and [NiFeSe] hydrogenases) and those lacking nickel (the [Fe] hydrogenases).

The [NiFe] and [NiFeSe] hydrogenases are heterodimer that consist of a small subunit that contains a signal peptide and a large subunit. All the known large subunits seem to be evolutionary related;[1] they contain two Cys-x-x-Cys motifs; one at their N-terminal end; the other at their C-terminal end. These four cysteines are involved in the binding of nickel.[2] In the [NiFeSe] hydrogenases the first cysteine of the C-terminal motif is a selenocysteine which has experimentally been shown to be a nickel ligand.[3]

References[edit]

  1. ^ Przybyla AE, Robbins J, Menon NK, Chatelus CY, Peck HD, Choi ES (1990). "Cloning and sequencing of a putative Escherichia coli [NiFe] hydrogenase-1 operon containing six open reading frames". J. Bacteriol. 172 (4): 1969–1977. doi:10.1128/jb.172.4.1969-1977.1990. PMC 208693. PMID 2180913.
  2. ^ Volbeda A, Hatchikian EC, Piras C, Frey M, Fontecilla-Camps JC, Charon MH (1995). "Crystal structure of the nickel-iron hydrogenase from Desulfovibrio gigas". Nature. 373 (6515): 580–587. doi:10.1038/373580a0. PMID 7854413. S2CID 4335445.
  3. ^ Moura I, Eidsness MK, Scott RA, Moura JJ, Legall J, Peck Jr HD, Prickril BC, DerVartanian DV (1989). "Evidence for selenocysteine coordination to the active site nickel in the [NiFeSe]hydrogenases from Desulfovibrio baculatus". Proc. Natl. Acad. Sci. U.S.A. 86 (1): 147–151. doi:10.1073/pnas.86.1.147. PMC 286421. PMID 2521386.
This article incorporates text from the public domain Pfam and InterPro: IPR001501