Iron-containing proteins in Chromatium. II. Purification and properties of cholate-solubilized cytochrome complex

Stephen Kennel, M. D. Kamen

Research output: Contribution to journalArticle

39 Citations (Scopus)

Abstract

A cytochrome complex was solubilized from the membrane fraction of Chromatium and purified by chromatography on hydroxylapatite. The purified cytochrome contained two different redox potential heme moieties: c-556 (+325 mV), and c-552.5 (+8 mV). The detergent-solubilized cytochrome was found to be identical to the membrane-bound form with respect to spectra, redox potentials, and absence of CO-binding capacity. Assuming a ratio of 1 c-556 : 2 c-552.5 in the complex, the reduced-oxidized absorption constants for the two spectral forms are: high potential cytochrome, εred-ox (556 nm) = 15.1 mM-1 and εred-ox (442 nm) = 103 mM-1; low potential cytochrome, εred-ox (552.5 nm) = 13.1 mM-1 and εred-ox (423.5 nm) = 89 mM-1. The spectral and chemical properties of the cytochrome complex show that none of the buffer-soluble cytochromes can be identified with this cytochrome complex.

Original languageEnglish (US)
Pages (from-to)153-166
Number of pages14
JournalBBA - Bioenergetics
Volume253
Issue number1
DOIs
StatePublished - Nov 2 1971

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Chromatium
Cholates
Cytochromes
Purification
Iron
Proteins
Oxidation-Reduction
Membranes
Durapatite
Carbon Monoxide
Chromatography
Heme
Detergents
Chemical properties
Buffers

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Cell Biology

Cite this

Iron-containing proteins in Chromatium. II. Purification and properties of cholate-solubilized cytochrome complex. / Kennel, Stephen; Kamen, M. D.

In: BBA - Bioenergetics, Vol. 253, No. 1, 02.11.1971, p. 153-166.

Research output: Contribution to journalArticle

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N2 - A cytochrome complex was solubilized from the membrane fraction of Chromatium and purified by chromatography on hydroxylapatite. The purified cytochrome contained two different redox potential heme moieties: c-556 (+325 mV), and c-552.5 (+8 mV). The detergent-solubilized cytochrome was found to be identical to the membrane-bound form with respect to spectra, redox potentials, and absence of CO-binding capacity. Assuming a ratio of 1 c-556 : 2 c-552.5 in the complex, the reduced-oxidized absorption constants for the two spectral forms are: high potential cytochrome, εred-ox (556 nm) = 15.1 mM-1 and εred-ox (442 nm) = 103 mM-1; low potential cytochrome, εred-ox (552.5 nm) = 13.1 mM-1 and εred-ox (423.5 nm) = 89 mM-1. The spectral and chemical properties of the cytochrome complex show that none of the buffer-soluble cytochromes can be identified with this cytochrome complex.

AB - A cytochrome complex was solubilized from the membrane fraction of Chromatium and purified by chromatography on hydroxylapatite. The purified cytochrome contained two different redox potential heme moieties: c-556 (+325 mV), and c-552.5 (+8 mV). The detergent-solubilized cytochrome was found to be identical to the membrane-bound form with respect to spectra, redox potentials, and absence of CO-binding capacity. Assuming a ratio of 1 c-556 : 2 c-552.5 in the complex, the reduced-oxidized absorption constants for the two spectral forms are: high potential cytochrome, εred-ox (556 nm) = 15.1 mM-1 and εred-ox (442 nm) = 103 mM-1; low potential cytochrome, εred-ox (552.5 nm) = 13.1 mM-1 and εred-ox (423.5 nm) = 89 mM-1. The spectral and chemical properties of the cytochrome complex show that none of the buffer-soluble cytochromes can be identified with this cytochrome complex.

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