Ubiquinol-Cytochrome c Oxidoreductase
نویسندگان
چکیده
منابع مشابه
Cytochrome electron spin resonance line shapes, ligand fields, and components stoichiometry in ubiquinol-cytochrome c oxidoreductase.
The EPR spectra of the cytochromes in ubiquinol-cytochrome c oxidoreductase (Complex III) have peaks at g = 3.78 (cytochrome b566) g = 3.45 (cytochrome b562) and g = 3.35 (cytochrome c1). The highly asymmetric peak of cytochrome b566 has been simulated using an arbitrary gaussian distribution of crystal field parameters. The asymmetry is due to the nonlinear relationship between field position ...
متن کاملTopological organization of subunits VII and VIII in the ubiquinol-cytochrome c oxidoreductase of Saccharomyces cerevisiae.
To determine the topology of subunit VIII of the yeast ubiquinol-cytochrome c oxidoreductase in the mitochondrial inner membrane, an epitope has been introduced in the N-terminal half of this protein. Previous topology studies had shown that at least the C-terminus faces the intermembrane space [Hemrika and Berden (1990) Eur. J. Biochem. 192, 761-765]. Based on sensitivity of the protein to pro...
متن کاملDecreased NADH dehydrogenase and ubiquinol-cytochrome c oxidoreductase in peripheral arterial disease.
Peripheral arterial disease (PAD) is associated with muscle metabolic changes that may contribute to the disability in these patients. However, the biochemical defects in PAD have not been identified. The present study was undertaken to test the hypothesis that PAD is associated with specific defects in skeletal muscle electron transport chain activity. Seventeen patients with PAD and nine age-...
متن کاملPurification of a three-subunit ubiquinol-cytochrome c oxidoreductase complex from Paracoccus denitrificans.
A ubiquinol-cytochrome c oxidoreductase (cytochrome bc1) complex has been purified from the plasma membrane of aerobically grown Paracoccus denitrificans by extraction with dodecyl maltoside and ion exchange chromatography of the extract. The purified complex contains two spectrally and thermodynamically distinct b cytochromes, cytochrome c1, and a Rieske-type iron-sulfur protein. Optical spect...
متن کاملAspartate-187 of cytochrome b is not needed for DCCD inhibition of ubiquinol: cytochrome c oxidoreductase in Rhodobacter sphaeroides chromatophores.
N,N'-dicyclohexylcarbodiimide (DCCD) has been reported to inhibit steady-state proton translocation by cytochrome bc(1) and b(6)f complexes without significantly altering the rate of electron transport, a process referred to as decoupling. In chromatophores of the purple bacterium Rhodobacter sphaeroides, this has been associated with the specific labeling of a surface-exposed aspartate-187 of ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1996
ISSN: 0021-9258
DOI: 10.1074/jbc.271.11.6164