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Formaldehyde Ferredoxin Oxidoreductase

Part 5. Molybdenum/Tungsten

  1. Roopali Roy1,
  2. Ish K Dhawan2,
  3. Michael K Johnson2,
  4. Douglas C Rees3,
  5. Michael WW Adams1

Published Online: 15 APR 2006

DOI: 10.1002/0470028637.met179

Handbook of Metalloproteins

Handbook of Metalloproteins

How to Cite

Roy, R., Dhawan, I. K., Johnson, M. K., Rees, D. C. and Adams, M. W. 2006. Formaldehyde Ferredoxin Oxidoreductase. Handbook of Metalloproteins. 5.

Author Information

  1. 1

    University of Georgia, Department of Biochemistry and Molecular Biology, Athens, USA

  2. 2

    University of Georgia, Department of Chemistry, Athens, USA

  3. 3

    California Institute of Technology, Department of Chemistry and Chemical Engineering, Pasadena, USA

Publication History

  1. Published Online: 15 APR 2006

Abstract

Formaldehyde ferredoxin oxidoreductase (FOR) is a homotetramer where each subunit contains a [4Fe–4S] cluster and a mononuclear tungsten atom coordinated by the dithioline groups of two pterin molecules. It is a member of a family of five closely related tungstoenzymes found in organisms that grow at high temperatures in marine volcanic vents. FOR catalyzes the two-electron oxidation of its aldehyde substrate to the corresponding acid with the concomitant reduction of ferredoxin, its physiological electron acceptor. FOR oxidizes short chain C1-C4 aldehydes as substrates but has the highest affinity for C4-C6 di- and semialdehydes. The enzyme is proposed to have a role in peptide metabolism.

3D Structure

Keywords:

  • tungsten;
  • tungsten-containing enzyme;
  • formaldehyde oxidoreductase;
  • iron-sulfur cluster;
  • pterin cofactor;
  • pyrococcus furiosus;
  • thermococcus litoralis;
  • semialdehyde oxidation;
  • hyperthermophile;
  • ferredoxin