Sodium Ions Affect the pH behavior of the Soluble Hydrogenase of Alcaligenes Eutrophus H16

Abstract

Hydrogenase activity of the soluble hydrogenase from Alcaligenes eutrophus H16 was inhibited by monovalent cations in the order Na+>Li+>K+>NH4+>Cs+. Hydrogenase activity was also slightly inhibited by monovalent anions. The Na(+) -induced inhibition was not altered with varying NAD+ or H2 concentrations, suggesting that Na+ ions do not interfere with substrate binding. The inhibition was lowered when the H+ concentration was increased over a range of pH 8.5 to 7.0. Examination of the pH-velocity curve shows that NaC1 lowers and shifts the pH optimum in the acidic direction. These data suggest that Na+ ions bind to the enzyme, perhaps displacing protons.

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Document Details

Document Type
Technical Report
Publication Date
Jan 01, 1993
Accession Number
ADA268228

Entities

People

  • A. L. Harabin
  • B. Tyree
  • J. R. Dejesus
  • K. K. Kumaroo

Organizations

  • Naval Medical Research Center

Tags

DTIC Thesaurus Topics

  • Biomedical Research
  • Cells
  • Chemical Compounds
  • Classification
  • Cyanides
  • Demographic Cohorts
  • Electrodes
  • Government Procurement
  • Governments
  • Hydrogen
  • Hydrogen Electrodes
  • Inhibition
  • Inhibitors
  • Laboratory Animals
  • Materials
  • Security
  • Technical Information Centers

Fields of Study

  • Biology

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  • Materials Science and Engineering.
  • Military Engineering.
  • Molecular and Cellular Biochemistry