Interaction between adrenodoxin and cytochrome c.

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Fluorescence energy transfer studies of the interaction between adrenodoxin and cytochrome c.

The interaction between beef adrenodoxin and horse heart cytochrome c was studied by measuring the fluorescence emission of the single tyrosine at residue 82 of adrenodoxin. Addition of cytochrome c at low ionic strength (5 n m sodium morpholinosulfonate, pH 7.5) decreased the 331 nm fluorescence consistent with the formation of a 1:l adrenodoxin-cytochrome c complex with a dissociation constan...

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Adrenodoxin interaction with adrenodoxin reductase and cytochrome P-450scc. Cross-linking of protein complexes and effects of adrenodoxin modification by 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide.

Modification of the three carboxyl groups on adrenodoxin using a water-soluble carbodiimide (1-ethyl-3-(3-dimethylaminopropyl)carbodiimide) caused a weakening of the binding of this iron-sulfur protein to both its electron donor protein, adrenodoxin reductase, and its electron acceptor protein, cytochrome P-450scc. Based upon the proximity of the modified groups, the site on adrenodoxin for int...

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Interaction of myoglobin and cytochrome C.

Spectrophotometric studies of various mixtures of reduced and oxidized forms of myoglobin and cytochrome c revealed that oxymyoglobin is capable of reducing ferricytochrome c at a molar ratio of 1. Other combinations, i.e. oxymyoglobin and ferrocytochrome c; metmyoglobin and ferricytochrome c; or metmyoglobin and ferrocytochrome c showed no spectral change during the time course studied. The pH...

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Interaction of Myoglobin and Cytochrome c*

Spectrophotometric studies of various mixtures of reduced and oxidized forms of myoglobin and cytochrome c revealed that oxymyoglobin is capable of reducing ferricytochrome c at a molar ratio of 1. Other combinations, i.e. oxymyoglobin and ferrocytochrome c; metmyoglobin and ferricytochrome c; or metmyoglobin and ferrocytochrome c showed no spectral change during the time course studied. The pH...

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Mechanism of peroxynitrite interaction with cytochrome c.

Kinetics of the reaction of peroxynitrite with ferric cytochrome c in the absence and presence of bicarbonate was studied. It was found that the heme iron in ferric cytochrome c does not react directly with peroxynitrite. The rates of the absorbance changes in the Soret region of cytochrome c spectrum caused by peroxynitrite or peroxynitrite/bicarbonate were the same as the rate of spontaneous ...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1981

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(19)69333-6