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Related Experiment Videos

Molybdenum oxidation by Thiobacillus ferrooxidans.

T Sugio1, K Hirayama, K Inagaki

  • 1Department of Biological Function and Genetic Resources Science and Department of Bioresources Chemistry, Faculty of Agriculture, Okayama University, 1-1-1 Tsushima Naka, Okayama 700, Japan.

Applied and Environmental Microbiology
|May 1, 1992
PubMed
Summary

Thiobacillus ferrooxidans AP19-3 utilizes a plasma membrane-bound molybdenum oxidase for enzymatic oxidation of molybdenum blue. This enzyme, a cytochrome oxidase, plays a crucial role in the oxidation process.

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Area of Science:

  • Microbiology
  • Biochemistry
  • Environmental Science

Background:

  • Thiobacillus ferrooxidans AP19-3 is known for its metabolic capabilities.
  • Molybdenum oxidation is an important biogeochemical process.

Purpose of the Study:

  • To investigate the enzymatic oxidation of molybdenum blue by Thiobacillus ferrooxidans AP19-3.
  • To purify and characterize the enzyme responsible for this oxidation.

Main Methods:

  • Enzymatic assays on Thiobacillus ferrooxidans AP19-3.
  • Purification of molybdenum oxidase from bacterial plasma membranes.
  • Spectroscopic analysis of the purified enzyme.
  • Enzyme activity inhibition studies.

Main Results:

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  • Molybdenum oxidase was purified 77-fold from cell extracts.
  • The purified enzyme exhibited absorption maxima characteristic of reduced-type cytochrome oxidase.
  • Optimum pH for molybdenum oxidase activity was 5.5.
  • Enzyme activity was inhibited by sodium cyanide and carbon monoxide.
  • Molybdenum blue reduced the oxidized cytochrome oxidase, confirming its role.

Conclusions:

  • A plasma membrane-bound molybdenum oxidase, a cytochrome oxidase, is responsible for the enzymatic oxidation of molybdenum blue in Thiobacillus ferrooxidans AP19-3.
  • Cytochrome oxidase is essential for the molybdenum blue oxidation pathway.
  • The findings contribute to understanding microbial metabolism and biogeochemical cycling of molybdenum.