Display Settings:

Format

Send to:

Choose Destination
J Mol Microbiol Biotechnol. 2005;10(2-4):92-104.

Energy-converting [NiFe] hydrogenases: more than just H2 activation.

Author information

  • 1Max-Planck-Institut für terrestrische Mikrobiologie, Marburg, Germany. hedderic@staff.uni-marburg.de

Abstract

The well-characterized [NiFe] hydrogenases have a key function in the H2 metabolism of various microorganisms. A subfamily of the [NiFe] hydrogenases with unique properties has recently been identified. The six conserved subunits that build the core of these membrane-bound hydrogenases share sequence similarity with subunits that form the catalytic core of energy-conserving NADH:quinone oxidoreductases (complex I). The physiological role of some of these hydrogenases is to catalyze the reduction of H+ with electrons derived from reduced ferredoxins or polyferredoxins. This exergonic reaction is coupled to energy conservation by means of electron-transport phosphorylation. Other members of this hydrogenase subfamily mainly function in providing the cell with reduced ferredoxin using H2 as electron donor in a reaction driven by reverse electron transport. These hydrogenases have therefore been designated as energy-converting [NiFe] hydrogenases.

Copyright 2005 S. Karger AG, Basel.

PMID:
16645307
[PubMed - indexed for MEDLINE]
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for S. Karger AG, Basel, Switzerland
    Loading ...
    Write to the Help Desk