Kinetic and thermodynamic resolution of cytochrome c 1 and cytochrome c 2 from Rhodopseudomonas sphaeroides
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چکیده
منابع مشابه
Cytochrome c-mediated electron transfer between ubiquinol-cytochrome c reductase and cytochrome c oxidase. Kinetic evidence for a mobile cytochrome c pool.
Ubiquinol oxidase has been reconstituted from ubiquinol-cytochrome c reductase (Complex III), cytochrome c and cytochrome c oxidase (Complex IV). The steady-state level of reduction of cytochrome c by ubiquinol-2 varies with the molar ratios of the complexes and with the presence of antimycin in a way that can be quantitatively accounted for by a model in which cytochrome c acts as a freely dif...
متن کاملDefinition of the interaction domain for cytochrome c on cytochrome c oxidase. Ii. Rapid kinetic analysis of electron transfer from cytochrome c to Rhodobacter sphaeroides cytochrome oxidase surface mutants.
The reaction between cytochrome c (Cc) and Rhodobacter sphaeroides cytochrome c oxidase (CcO) was studied using a cytochrome c derivative labeled with ruthenium trisbipyridine at lysine 55 (Ru-55-Cc). Flash photolysis of a 1:1 complex between Ru-55-Cc and CcO at low ionic strength results in electron transfer from photoreduced heme c to Cu(A) with an intracomplex rate constant of k(a) = 4 x 10(...
متن کاملQuantitative resolution of succinate-cytochrome c reductase into succinate-ubiquinone and ubiquinol-cytochrome c reductases.
A purified, active succinate-ubiquinone reductase was prepared from succinate-cytochrome c reductase without damage to ubiquinol-cytochrome c reductase by 1.1% Triton X-100 solubilization at pH 8.0, and calcium phosphate column chromatography in 50 mM Tris-succinate buffer, pH 8.0, containing 30 mM potassium phosphate. Succinate-ubiquinone reductase thus obtained contains ubiquinone and catalyz...
متن کاملKinetic studies on [methionine sulphoxide] cytochrome c.
A cytochrome c haem ligand, methionine-80, was photo-oxidized to methionine sulphoxide and the subsequent changes in redox properties and ligand binding were monitored kinetically. Isoelectric focusing of the product showed the presence of a single oxidized species, capable of binding CO when reduced. The binding of CO to the reduced protein was followed in stopped-flow experiments, which revea...
متن کاملReduction and activity of cytochrome c in the cytochrome c-cytochrome aa3 complex.
Uncharged reductants, such as NNN'N'-tetramethyl-p-phenylenediamine and diaminodurene, reduce cytochrome c at both high and low ionic strength, unlike ascorbate, which is effective only at low ionic strength. The 'tightly bound' cytochrome c-cytochrome c oxidase complex, with 1 equiv. of cytochrome c per cytochrome aa3, can be prepared by simple mixing of the two component species. Its properti...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1982
ISSN: 0014-5793
DOI: 10.1016/0014-5793(82)81105-8