Characterization of two different 2-oxoglutarate:ferredoxin oxidoreductases from Hydrogenobacter thermophilus TK-6

Biochem Biophys Res Commun. 2003 Dec 26;312(4):1297-302. doi: 10.1016/j.bbrc.2003.11.078.

Abstract

A thermophilic, chemolithoautotrophic hydrogen-oxidizing bacterium, Hydrogenobacter thermophilus TK-6, fixes carbon dioxide via the reductive TCA cycle. 2-Oxoglutarate:ferredoxin oxidoreductase (OGOR) is one of the key enzymes of this cycle. Strain TK-6 has two distinct OGOR enzymes termed For and Kor. These enzymes were purified and characterized following heterologous expression in Escherichia coli. The specific activity of For was approximately one-tenth of that of Kor. Additionally, For showed higher thermo-stability than Kor under both aerobic and anaerobic conditions. Western blot analysis showed that both of For and Kor were expressed when strain TK-6 was grown under aerobic conditions. In contrast, only Kor was expressed when the strain was grown under anaerobic conditions using nitrate as a terminal electron acceptor. These results indicate that For supports the optimal growth of strain TK-6 in the presence of oxygen.

Publication types

  • Comparative Study

MeSH terms

  • Bacteria / chemistry*
  • Bacteria / enzymology*
  • Bacteria, Aerobic / chemistry
  • Bacteria, Aerobic / enzymology
  • Bacteria, Anaerobic / chemistry
  • Bacteria, Anaerobic / metabolism
  • Citric Acid Cycle / physiology
  • Enzyme Activation
  • Enzyme Stability
  • Gene Expression Regulation, Bacterial / physiology*
  • Gene Expression Regulation, Enzymologic / physiology*
  • Hydrogen-Ion Concentration
  • Ketone Oxidoreductases / chemistry*
  • Ketone Oxidoreductases / classification
  • Ketone Oxidoreductases / genetics
  • Ketone Oxidoreductases / metabolism*
  • Molecular Weight
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism
  • Species Specificity
  • Temperature

Substances

  • Recombinant Proteins
  • Ketone Oxidoreductases
  • 2-oxoglutarate synthase