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

Tetsuya Ono, Masaharu Ishii, Ki Suk 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

Fingerprint

Hydrogenase
Pseudomonas
Purification
Hydrogen
Bacteria
Membranes
Cell growth
Durapatite
Acetone
Atmosphere
Amino Acid Sequence
Gases
Amino Acids
Peptides
Temperature
Enzymes
Growth
iron hydrogenase

All Science Journal Classification (ASJC) codes

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

Cite this

Purification and Characterization of Membrane-bound Hydrogenase from a Thermophilic Hydrogen-Oxidizing Bacterium, Pseudomonas hydrogenothermophila Strain TH-1. / Ono, Tetsuya; Ishii, Masaharu; Yoon, Ki Suk; Igarashi, Yasuo; Kodama, Tohru.

In: Bioscience, Biotechnology, and Biochemistry, Vol. 59, No. 5, 01.01.1995, p. 917-919.

Research output: Contribution to journalArticle

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