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Cell Mol Life Sci. 2007 May;64(9):1063-84.

[FeFe] hydrogenases and their evolution: a genomic perspective.

Author information

1
Chimie et Biologie des Métaux, UMR 5249 CEA-CNRS-UJF, IRTSV, CEA-Grenoble, 38054 Grenoble, France. jacques.meyer@cea.fr

Abstract

Most hydrogenases (H2ases), the enzymes that produce or oxidize dihydrogen, possess dimetallic active sites and belong to either one of two phylogenetically distinct classes, the [NiFe] and the [FeFe] H2ases. These families of H2ases share a number of similarities regarding active site structure and reaction mechanism, as a result of convergent evolution. They are otherwise alien to each other, in particular with respect to protein sequence and structure, maturation mechanisms, and distribution among the realms of life. One of the interesting features of [FeFe] H2ases is their occurrence in anaerobic bacteria, anaerobic protists, and mitochondriate eukaryotes. They thus have the potential to report on important evolutionary events, including transitions from the prokaryote to the eukaryote lifestyle. Genome sequences yield a variety of [FeFe] H2ase sequences that have been implemented to shed light on the evolution of these proteins and their host organisms.

PMID:
17353991
DOI:
10.1007/s00018-007-6477-4
[Indexed for MEDLINE]

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