JBIC Journal of Biological Inorganic Chemistry

, Volume 9, Issue 7, pp 791–799

Mo and W bis-MGD enzymes: nitrate reductases and formate dehydrogenases

  • José J. G. Moura
  • Carlos D. Brondino
  • José Trincão
  • Maria João Romão

DOI: 10.1007/s00775-004-0573-9

Cite this article as:
Moura, J.J.G., Brondino, C.D., Trincão, J. et al. J Biol Inorg Chem (2004) 9: 791. doi:10.1007/s00775-004-0573-9


Molybdenum and tungsten are second- and third-row transition elements, respectively, which are found in a mononuclear form in the active site of a diverse group of enzymes that generally catalyze oxygen atom transfer reactions. Mononuclear Mo-containing enzymes have been classified into three families: xanthine oxidase, DMSO reductase, and sulfite oxidase. The proteins of the DMSO reductase family present the widest diversity of properties among its members and our knowledge about this family was greatly broadened by the study of the enzymes nitrate reductase and formate dehydrogenase, obtained from different sources. We discuss in this review the information of the better characterized examples of these two types of Mo enzymes and W enzymes closely related to the members of the DMSO reductase family. We briefly summarize, also, the few cases reported so far for enzymes that can function either with Mo or W at their active site.


DMSO reductase familyFormate dehydrogenaseMolybdenum-containing enzymesNitrate reductaseTungsten-containing enzymes



aldehyde oxidoreductase


dimethyl sulfoxide


extended X-ray absorption fine structure


formate dehydrogenase


formate dehydrogenase component of the formate-hydrogen lyase complex of E. coli


nitrate-dependent formate dehydrogenase of E. coli when growing anaerobically on nitrate


pterin cofactor with a guanine dinucleotide


periplasmic nitrate reductase


respiratory nitrate reductase


sulfate reducing bacteria


trimethylamine N-oxide

Copyright information

© SBIC 2004

Authors and Affiliations

  • José J. G. Moura
    • 1
  • Carlos D. Brondino
    • 1
    • 2
  • José Trincão
    • 1
  • Maria João Romão
    • 1
  1. 1.REQUIMTE/CQFB, Departamento de Química, Faculdade de Ciências e TecnologiaUniversidade Nova de LisboaCaparicaPortugal
  2. 2.Facultad de Bioquímica y Ciencias BiológicasUniversidad Nacional del LitoralSanta FeArgentina