Purification and Characterization of Membrane-bound Hydrogenase from a Thermophilic Hydrogen-Oxidizing Bacterium, Pseudomonas hydrogenothermophila Strain TH-1

Tetsuya Ono, Masaharu Ishii, Ki Seok Yoon, Yasuo Igarashi, Tohru Kodama

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

A membrane-bound hydrogenase was purified aerobically by one step using a hydroxyapatite column after solubilization by acetone treatment from a thermophilic hydrogen-oxidizing bacterium, Pseudomonas hydrogenothermophila strain TH-1. The enzyme consists of two polypeptides of 63 and 31 kDa, respectively. The amino-terminal amino acid sequences of both subunits were homologous to membrane-bound type [Ni-Fe] hydrogenases from other origins. The thermostability under a hydrogen gas atmosphere is highly stable at 50°C, which is the optimum temperature for the cell growth.

Original languageEnglish
Pages (from-to)917-919
Number of pages3
JournalBioscience, biotechnology, and biochemistry
Volume59
Issue number5
DOIs
Publication statusPublished - Jan 1 1995
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Analytical Chemistry
  • Biochemistry
  • Applied Microbiology and Biotechnology
  • Molecular Biology
  • Organic Chemistry

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