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

doi:10.1271/bbb.59.917

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 journal › Article › peer-review

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 language	English
Pages (from-to)	917-919
Number of pages	3
Journal	Bioscience, biotechnology, and biochemistry
Volume	59
Issue number	5
DOIs	https://doi.org/10.1271/bbb.59.917
Publication status	Published - 1995
Externally published	Yes

All Science Journal Classification (ASJC) codes

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

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

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.",

author = "Tetsuya Ono and Masaharu Ishii and Yoon, {Ki Seok} and Yasuo Igarashi and Tohru Kodama",

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doi = "10.1271/bbb.59.917",

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AU - Ono, Tetsuya

AU - Ishii, Masaharu

AU - Yoon, Ki Seok

AU - Igarashi, Yasuo

AU - Kodama, Tohru

PY - 1995

Y1 - 1995

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JO - Bioscience, biotechnology, and biochemistry

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

Abstract

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