Recent progress in the Na(+)-translocating NADH-quinone reductase from the marine Vibrio alginolyticus

Biochim Biophys Acta. 2001 May 1;1505(1):37-44. doi: 10.1016/s0005-2728(00)00275-9.

Abstract

The respiratory chain of Gram-negative marine and halophilic bacteria has a Na(+)-dependent NADH-quinone reductase that functions as a primary Na(+) pump. The Na(+)-translocating NADH-quinone reductase (NQR) from the marine Vibrio alginolyticus is composed of six structural genes (nqrA to nqrF). The NqrF subunit has non-covalently bound FAD. There are conflicting results on the existence of other flavin cofactors. Recent studies revealed that the NqrB and NqrC subunits have a covalently bound flavin, possibly FMN, which is attached to a specified threonine residue. A novel antibiotic, korormicin, was found to specifically inhibit the NQR complex. From the homology search of the nqr operon, it was found that the Na(+)-pumping NQR complex is widely distributed among Gram-negative pathogenic bacteria.

Publication types

  • Review

MeSH terms

  • Amino Acid Sequence
  • Anti-Bacterial Agents / pharmacology
  • Bacterial Proteins / metabolism*
  • Cations, Monovalent
  • Electron Transport
  • Enzyme Inhibitors / pharmacology
  • Fatty Acids, Unsaturated / chemistry
  • Fatty Acids, Unsaturated / pharmacology
  • Lactones / chemistry
  • Lactones / pharmacology
  • Molecular Sequence Data
  • Oxidation-Reduction
  • Quinone Reductases / antagonists & inhibitors
  • Quinone Reductases / genetics
  • Quinone Reductases / metabolism*
  • Sodium / metabolism*
  • Vibrio / enzymology*
  • Water Microbiology

Substances

  • Anti-Bacterial Agents
  • Bacterial Proteins
  • Cations, Monovalent
  • Enzyme Inhibitors
  • Fatty Acids, Unsaturated
  • Lactones
  • korormicin
  • Sodium
  • sodium-translocating NADH-quinone reductase
  • Quinone Reductases