A new membrane-bound b-type cytochrome, cytochrome b-558, from photosynthetically grown Rhodopseudomonas sphaeroides

Koh Iba, Ken Ichiro Takamiya

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

A new membrane-bound b-type cytochrome, cytochrome b-558, was removed from chromatophore membranes of photosynthetically grown Rhodopseudomonas sphaeroides strain R-26 by deoxycholate-cholate extraction. The cytochrome was purified by ammonium sulfate fractionation and ion-exchange chromatography. Cytochrome b-558 had absorption maxima at 280 and 405 nm in the oxidized form, and at 558, 528, and 420 nm in the reduced form. It had a midpoint potential of -130 mV at pH 7.0. The minimal molecular weight of this protein was 42,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and it contained one mole heme per mole of protein. The isoelectric point was 8.5. The electrophoretic pattern of heme-carrying proteins and the redox potentiometry showed that cytochrome b-558 was present in membranes from wild type, strain R-26, and strain GA grown photosynthetically, but not from any strain grown aerobically.

Original languageEnglish
Pages (from-to)391-395
Number of pages5
JournalArchives of Biochemistry and Biophysics
Volume246
Issue number1
DOIs
Publication statusPublished - Jan 1 1986

Fingerprint

Cytochrome b Group
Rhodobacter sphaeroides
Membranes
Heme
Potentiometry
Chromatophores
Cholates
Proteins
Deoxycholic Acid
Ion Exchange Chromatography
Isoelectric Point
Ammonium Sulfate
Cytochromes
Sodium Dodecyl Sulfate
Oxidation-Reduction
Polyacrylamide Gel Electrophoresis
Fractionation
Chromatography
Molecular Weight
Electrophoresis

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology

Cite this

A new membrane-bound b-type cytochrome, cytochrome b-558, from photosynthetically grown Rhodopseudomonas sphaeroides. / Iba, Koh; Takamiya, Ken Ichiro.

In: Archives of Biochemistry and Biophysics, Vol. 246, No. 1, 01.01.1986, p. 391-395.

Research output: Contribution to journalArticle

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