Nickel-dependent hydrogenase

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Nickel-dependent hydrogenase
Identifiers
Symbol NiFeSe_Hases
Pfam PF00374
InterPro IPR001501
PROSITE PDOC00400
SCOP 1frv
SUPERFAMILY 1frv
TCDB 3.D.7

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. PMC 208693Freely accessible. 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. PMID 7854413. doi:10.1038/373580a0. 
  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. PMC 286421Freely accessible. PMID 2521386. doi:10.1073/pnas.86.1.147. 

This article incorporates text from the public domain Pfam and InterPro IPR001501