Purification and characterization of ferredoxin from hydrogenobacter thermophilus strain TK-6

Masaharu Ishii; Yasufumi Ueda; Ki Soek Yoon; Yasuo Igarashi; Tohru Kodama

doi:10.1271/bbb.60.1513

Purification and characterization of ferredoxin from hydrogenobacter thermophilus strain TK-6

Masaharu Ishii, Yasufumi Ueda, Ki Soek Yoon, Yasuo Igarashi, Tohru Kodama

Research output: Contribution to journal › Article › peer-review

8 Citations (Scopus)

Abstract

Ferredoxin was purified from cells of Hydrogenohacter thermophilus strain TK-6. Purification was performed aerobically by the addition of octyl-p-glucoside to the buffers. The purified ferredoxin had a molecular mass of 13,000 and contained a [4Fe-4S] cluster. The protein had a long stretch at the N-terminal region; however, the sequence was not similar to the sequences of ferredoxins with a long stretch from Archaehacteria.

Original language	English
Pages (from-to)	1513-1515
Number of pages	3
Journal	Bioscience, Biotechnology and Biochemistry
Volume	60
Issue number	9
DOIs	https://doi.org/10.1271/bbb.60.1513
Publication status	Published - Jan 1996
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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abstract = "Ferredoxin was purified from cells of Hydrogenohacter thermophilus strain TK-6. Purification was performed aerobically by the addition of octyl-p-glucoside to the buffers. The purified ferredoxin had a molecular mass of 13,000 and contained a [4Fe-4S] cluster. The protein had a long stretch at the N-terminal region; however, the sequence was not similar to the sequences of ferredoxins with a long stretch from Archaehacteria.",

author = "Masaharu Ishii and Yasufumi Ueda and Yoon, {Ki Soek} and Yasuo Igarashi and Tohru Kodama",

year = "1996",

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AU - Ishii, Masaharu

AU - Ueda, Yasufumi

AU - Yoon, Ki Soek

AU - Igarashi, Yasuo

AU - Kodama, Tohru

PY - 1996/1

Y1 - 1996/1

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AB - Ferredoxin was purified from cells of Hydrogenohacter thermophilus strain TK-6. Purification was performed aerobically by the addition of octyl-p-glucoside to the buffers. The purified ferredoxin had a molecular mass of 13,000 and contained a [4Fe-4S] cluster. The protein had a long stretch at the N-terminal region; however, the sequence was not similar to the sequences of ferredoxins with a long stretch from Archaehacteria.

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JO - Bioscience, Biotechnology and Biochemistry

JF - Bioscience, Biotechnology and Biochemistry

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ER -

Purification and characterization of ferredoxin from hydrogenobacter thermophilus strain TK-6

Abstract

All Science Journal Classification (ASJC) codes

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