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本文引用的文献

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The measurement of the cytochrome oxidase activity of enzyme preparations.酶制剂中细胞色素氧化酶活性的测定。
Biochem J. 1949;44(3):305-18. doi: 10.1042/bj0440305.
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Effect of haematin on the oxidation of succinic acid by tissue preparations.高铁血红素对组织制剂氧化琥珀酸的影响。
Biochem J. 1947;41(4):503-6. doi: 10.1042/bj0410503.
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Cytochemical studies. IV. Physical state of certain respiratory enzymes of mitochondria.细胞化学研究。IV. 线粒体某些呼吸酶的物理状态。
J Biol Chem. 1952 Feb;194(2):513-19.
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A microspectrophotometric method for the determination of cytochrome oxidase.一种测定细胞色素氧化酶的显微分光光度法。
J Biol Chem. 1951 Apr;189(2):665-70.
5
STUDIES ON CYTOCHROME OXIDASE. VI. KINETICS OF THE AEROBIC OXIDATION OF FERROCYTOCHROME C BY CYTOCHROME OXIDASE.细胞色素氧化酶研究。VI. 细胞色素氧化酶对亚铁细胞色素C的需氧氧化动力学
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The kinetics of cytochrome c oxidase. I. The system: cytochrome c-cytochrome oxidase-oxygen.细胞色素c氧化酶的动力学。I. 体系:细胞色素c-细胞色素氧化酶-氧气。
Biochim Biophys Acta. 1961 Jun 10;50:23-34. doi: 10.1016/0006-3002(61)91055-1.
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A study of the kinetics of the oxidation of cytochrome c by cytochrome c oxidase.细胞色素c氧化酶氧化细胞色素c的动力学研究。
Arch Biochem Biophys. 1956 Aug;63(2):403-13. doi: 10.1016/0003-9861(56)90055-8.
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A kinetic study of cytochrome oxidase.细胞色素氧化酶的动力学研究。
J Biol Chem. 1954 Aug;209(2):677-86.
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Ultramicrospectrophotometric determination of cytochrome oxidase for quantitative histochemistry.用于定量组织化学的细胞色素氧化酶的超微量分光光度测定法。
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10
Intracellular distribution of diphosphopyridine nucleotide-cytochrome c reductase and cytochrome c oxidase in mammalian brain.二磷酸吡啶核苷酸 - 细胞色素c还原酶和细胞色素c氧化酶在哺乳动物脑内的细胞内分布
J Biol Chem. 1952 Oct;198(2):821-6.

线粒体细胞色素c氧化酶催化亚铁细胞色素c氧化的单催化位点模型。

Single catalytic site model for the oxidation of ferrocytochrome c by mitochondrial cytochrome c oxidase.

作者信息

Speck S H, Dye D, Margoliash E

出版信息

Proc Natl Acad Sci U S A. 1984 Jan;81(2):347-51. doi: 10.1073/pnas.81.2.347.

DOI:10.1073/pnas.81.2.347
PMID:6320180
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC344673/
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.

摘要

提出了一个单一催化位点模型来解释细胞色素c氧化酶氧化亚铁细胞色素c的多相动力学(亚铁细胞色素c:氧氧化还原酶,EC 1.9.3.1)。该模型涉及底物与细胞色素c氧化酶上细胞色素c催化位点附近的位点发生非生产性结合,从而降低细胞色素c在催化位点的结合常数。这种底物抑制导致高铁细胞色素c-细胞色素c氧化酶复合物解离的一级速率常数增加,这是分光光度法测定中细胞色素c和细胞色素c氧化酶之间稳态电子传递的限速步骤,从而导致初始速率以及米氏常数增加——即多个动力学阶段。