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...

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Manylion Llyfryddiaeth
Prif Awduron: Errede, B, Haight, G P, Kamen, M D
Fformat: Erthygl
Iaith:en
Cyhoeddwyd: 1976
Pynciau:
Research Article
Mynediad Ar-lein:https://ncbi.nlm.nih.gov/pmc/articles/PMC335850/
https://ncbi.nlm.nih.gov/pubmed/174095
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spelling pubmed-3358502004-07-30 Oxidation of ferrocytochrome c by mitochondrial cytochrome c oxidase. Errede, B Haight, G P Kamen, M D Proc Natl Acad Sci U S A Research Article 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. Data adequate to derive such a rate expression are presented, as well as a method for estimation of constants which appear in the rate law deduced and reported herein. It is shown that either of two types of mechanisms, one assuming productive complex formation, as opposed to the other postulating dead-end complex formation, accurately predict the rate equation as deduced from experiment. 1976-01 /pmc/articles/PMC335850/ /pubmed/174095 Text en
institution US National Library of Medicine
collection PubMed Central
language en
format Article
topic Research Article
spellingShingle Research Article
Errede, B
Haight, G P
Kamen, M D
Oxidation of ferrocytochrome c by mitochondrial cytochrome c oxidase.
description 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. Data adequate to derive such a rate expression are presented, as well as a method for estimation of constants which appear in the rate law deduced and reported herein. It is shown that either of two types of mechanisms, one assuming productive complex formation, as opposed to the other postulating dead-end complex formation, accurately predict the rate equation as deduced from experiment.
author Errede, B
Haight, G P
Kamen, M D
author_facet Errede, B
Haight, G P
Kamen, M D
author_sort Errede, B
title Oxidation of ferrocytochrome c by mitochondrial cytochrome c oxidase.
title_short Oxidation of ferrocytochrome c by mitochondrial cytochrome c oxidase.
title_full Oxidation of ferrocytochrome c by mitochondrial cytochrome c oxidase.
title_fullStr Oxidation of ferrocytochrome c by mitochondrial cytochrome c oxidase.
title_full_unstemmed Oxidation of ferrocytochrome c by mitochondrial cytochrome c oxidase.
title_sort oxidation of ferrocytochrome c by mitochondrial cytochrome c oxidase.
publishDate 1976
url https://ncbi.nlm.nih.gov/pmc/articles/PMC335850/
https://ncbi.nlm.nih.gov/pubmed/174095
_version_ 1759617853458219008

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