Skip to main content
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1995 Aug;177(16):4817–4819. doi: 10.1128/jb.177.16.4817-4819.1995

Molecular characterization of the genes encoding the tungsten-containing aldehyde ferredoxin oxidoreductase from Pyrococcus furiosus and formaldehyde ferredoxin oxidoreductase from Thermococcus litoralis.

A Kletzin 1, S Mukund 1, T L Kelley-Crouse 1, M K Chan 1, D C Rees 1, M W Adams 1
PMCID: PMC177251  PMID: 7642512

Abstract

The hyperthermophilic archaea Pyrococcus furiosus and Thermococcus litoralis contain the tungstoenzymes aldehyde ferredoxin oxidoreductase, a homodimer, and formaldehyde ferredoxin oxidoreductase, a homotetramer. herein we report the cloning and sequencing of the P. furiosus gene aor (605 residues; M(r), 66,630) and the T. litoralis gene for (621 residues; M(r), 68,941).

Full Text

The Full Text of this article is available as a PDF (410.9 KB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Bertram P. A., Karrasch M., Schmitz R. A., Böcher R., Albracht S. P., Thauer R. K. Formylmethanofuran dehydrogenases from methanogenic Archaea. Substrate specificity, EPR properties and reversible inactivation by cyanide of the molybdenum or tungsten iron-sulfur proteins. Eur J Biochem. 1994 Mar 1;220(2):477–484. doi: 10.1111/j.1432-1033.1994.tb18646.x. [DOI] [PubMed] [Google Scholar]
  2. Chan M. K., Mukund S., Kletzin A., Adams M. W., Rees D. C. Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase. Science. 1995 Mar 10;267(5203):1463–1469. doi: 10.1126/science.7878465. [DOI] [PubMed] [Google Scholar]
  3. Heider J., Ma K., Adams M. W. Purification, characterization, and metabolic function of tungsten-containing aldehyde ferredoxin oxidoreductase from the hyperthermophilic and proteolytic archaeon Thermococcus strain ES-1. J Bacteriol. 1995 Aug;177(16):4757–4764. doi: 10.1128/jb.177.16.4757-4764.1995. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Mukund S., Adams M. W. Characterization of a novel tungsten-containing formaldehyde ferredoxin oxidoreductase from the hyperthermophilic archaeon, Thermococcus litoralis. A role for tungsten in peptide catabolism. J Biol Chem. 1993 Jun 25;268(18):13592–13600. [PubMed] [Google Scholar]
  5. Mukund S., Adams M. W. Characterization of a tungsten-iron-sulfur protein exhibiting novel spectroscopic and redox properties from the hyperthermophilic archaebacterium Pyrococcus furiosus. J Biol Chem. 1990 Jul 15;265(20):11508–11516. [PubMed] [Google Scholar]
  6. Mukund S., Adams M. W. Glyceraldehyde-3-phosphate ferredoxin oxidoreductase, a novel tungsten-containing enzyme with a potential glycolytic role in the hyperthermophilic archaeon Pyrococcus furiosus. J Biol Chem. 1995 Apr 14;270(15):8389–8392. doi: 10.1074/jbc.270.15.8389. [DOI] [PubMed] [Google Scholar]
  7. Mukund S., Adams M. W. The novel tungsten-iron-sulfur protein of the hyperthermophilic archaebacterium, Pyrococcus furiosus, is an aldehyde ferredoxin oxidoreductase. Evidence for its participation in a unique glycolytic pathway. J Biol Chem. 1991 Aug 5;266(22):14208–14216. [PubMed] [Google Scholar]
  8. Thoenes U., Flores O. L., Neves A., Devreese B., Van Beeumen J. J., Huber R., Romão M. J., LeGall J., Moura J. J., Rodrigues-Pousada C. Molecular cloning and sequence analysis of the gene of the molybdenum-containing aldehyde oxido-reductase of Desulfovibrio gigas. The deduced amino acid sequence shows similarity to xanthine dehydrogenase. Eur J Biochem. 1994 Mar 15;220(3):901–910. doi: 10.1111/j.1432-1033.1994.tb18693.x. [DOI] [PubMed] [Google Scholar]
  9. Trautwein T., Krauss F., Lottspeich F., Simon H. The (2R)-hydroxycarboxylate-viologen-oxidoreductase from Proteus vulgaris is a molybdenum-containing iron-sulphur protein. Eur J Biochem. 1994 Jun 15;222(3):1025–1032. doi: 10.1111/j.1432-1033.1994.tb18954.x. [DOI] [PubMed] [Google Scholar]
  10. White H., Feicht R., Huber C., Lottspeich F., Simon H. Purification and some properties of the tungsten-containing carboxylic acid reductase from Clostridium formicoaceticum. Biol Chem Hoppe Seyler. 1991 Nov;372(11):999–1005. doi: 10.1515/bchm3.1991.372.2.999. [DOI] [PubMed] [Google Scholar]
  11. White H., Strobl G., Feicht R., Simon H. Carboxylic acid reductase: a new tungsten enzyme catalyses the reduction of non-activated carboxylic acids to aldehydes. Eur J Biochem. 1989 Sep 1;184(1):89–96. doi: 10.1111/j.1432-1033.1989.tb14993.x. [DOI] [PubMed] [Google Scholar]
  12. Yamamoto I., Saiki T., Liu S. M., Ljungdahl L. G. Purification and properties of NADP-dependent formate dehydrogenase from Clostridium thermoaceticum, a tungsten-selenium-iron protein. J Biol Chem. 1983 Feb 10;258(3):1826–1832. [PubMed] [Google Scholar]

Articles from Journal of Bacteriology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES