Oxidation of ferrocytochrome c by mitochondrial cytochrome c oxidase.
نویسندگان
چکیده
منابع مشابه
Oxidation of ferrocytochrome c by mitochondrial cytochrome c oxidase.
Attempts to rationalize the kinetics of cytochrome c oxidation catalyzed by solubilized mitochondrial cytochrome c oxidase (ferrocytochrome c:oxygen oxidoreductase, EC 1.9.3.1) have been based on assumptions of productive complex formation (Michaelis-Menten approach). However, the range of substrate concentrations used has not, in general, been sufficient to establish a general rate equation. D...
متن کاملSingle catalytic site model for the oxidation of ferrocytochrome c by mitochondrial cytochrome c oxidase.
A single catalytic site model is proposed to account for the multiphasic kinetics of oxidation of ferrocytochrome c by cytochrome c oxidase (ferrocytochrome c:oxygen oxidoreductase, EC 1.9.3.1). This model involves nonproductive binding of substrate to sites near the catalytic site on cytochrome c oxidase for cytochrome c, decreasing the binding constant for cytochrome c at the catalytic site. ...
متن کاملStudies on Cytochrome Oxidase. Vi. Kinetics of the Aerobic Oxidation of Ferrocytochrome C by Cytochrome Oxidase.
The rate of reaction can be determined by measuring the rate of either oxygen consumption or ferrocytochrome c oxidation. When the rate of oxygen consumption is measured either manometrically or polarographically, a mixture of a limited amount of cytochrome c and an excess of reducing agent, instead of excess ferrocytochrome c, is used as an electron donor system. In this case the true electron...
متن کاملIon and pH Optimum for the Oxidation of Ferrocytochrome c by Cytochrome c Oxidase in A’ II?
It has been established by a number of investigators that definition of the pH optimum (in addition to the temperature and the concentration of the substrate and the enzyme) without specification of the ion species or its activity does not fully characterize an enzyme reaction. For example, as early as 1934, Howell and Sumner (1) showed that the pH optimum of urease activity was dependent on th...
متن کاملThe cytochrome c peroxidase-catalyzed oxidation of ferrocytochrome c by hydrogen peroxide. Steady state kinetic mechanism.
Initial velocities for the cytochrome c peroxidase-catalyzed oxidation of ferrocytochrome c by hydrogen peroxide have been measured as functions of both the ferrocytochrome c (0.27-104 microM) and hydrogen peroxide (0.25-200 microM) concentrations at 25 degrees C, 0.01 M ionic strength, and pH 7 in a cacodylate/KNO3 buffer system Eadie-Hofstee plots of the initial velocity as a function of ferr...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1976
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.73.1.113