Abstract:
: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. This substrate inhibition results in an increase in the first-order rate constant for the dissociation of the ferricytochrome c-cytochrome c oxidase complex, the rate-limiting step in the steady-state turnover of electrons between cytochrome c and cytochrome c oxidase in the spectrophotometric assay, yielding increases in the initial rate as well as the Michaelis constant--namely, multiple kinetic phases.
journal_name
Proc Natl Acad Sci U S Aauthors
Speck SH,Dye D,Margoliash Edoi
10.1073/pnas.81.2.347subject
Has Abstractpub_date
1984-01-01 00:00:00pages
347-51issue
2eissn
0027-8424issn
1091-6490journal_volume
81pub_type
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journal_title:Proceedings of the National Academy of Sciences of the United States of America
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