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 journalArticle

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 languageEnglish
Pages (from-to)1513-1515
Number of pages3
JournalBioscience, Biotechnology and Biochemistry
Volume60
Issue number9
DOIs
Publication statusPublished - Jan 1996

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Ferredoxins
Purification
Glucosides
Molecular mass
Buffers
Proteins

All Science Journal Classification (ASJC) codes

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

Cite this

Purification and characterization of ferredoxin from hydrogenobacter thermophilus strain TK-6. / Ishii, Masaharu; Ueda, Yasufumi; Yoon, Ki Soek; Igarashi, Yasuo; Kodama, Tohru.

In: Bioscience, Biotechnology and Biochemistry, Vol. 60, No. 9, 01.1996, p. 1513-1515.

Research output: Contribution to journalArticle

Ishii, Masaharu ; Ueda, Yasufumi ; Yoon, Ki Soek ; Igarashi, Yasuo ; Kodama, Tohru. / Purification and characterization of ferredoxin from hydrogenobacter thermophilus strain TK-6. In: Bioscience, Biotechnology and Biochemistry. 1996 ; Vol. 60, No. 9. pp. 1513-1515.
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