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Biochem J. 1977 Nov 15;168(2):133-9. doi: 10.1042/bj1680133.
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本文引用的文献

1
Protein measurement with the Folin phenol reagent.使用福林酚试剂进行蛋白质测定。
J Biol Chem. 1951 Nov;193(1):265-75.
2
Tricalcium phosphate as an adsorbent in the chromatography of proteins.磷酸三钙作为蛋白质色谱分析中的吸附剂。
Biochem J. 1951 Feb;48(2):171-4. doi: 10.1042/bj0480171.
3
Effect of triton X-100 and trypsin on NADPH-cytochrome C reductase reconstitutively active in fatty acid omega-hydroxylation.曲拉通X-100和胰蛋白酶对在脂肪酸ω-羟化中具有重组活性的NADPH-细胞色素C还原酶的影响。
FEBS Lett. 1972 Jan 15;20(1):105-107. doi: 10.1016/0014-5793(72)80028-0.
4
Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein).超氧化物歧化酶。红细胞铜蛋白(血铜蛋白)的酶功能。
J Biol Chem. 1969 Nov 25;244(22):6049-55.
5
The resolution and reconstitution of the liver microsomal hydroxylation system.肝脏微粒体羟化系统的分解与重组。
Biochim Biophys Acta. 1974 Sep 16;344(2):205-40. doi: 10.1016/0304-4157(74)90004-5.
6
Role of adrenochrome in aryl hydrocarbon hydroxylase induction by epinephrine in rat liver cell culture.肾上腺色素在大鼠肝细胞培养中肾上腺素诱导芳烃羟化酶中的作用。
Biochem Pharmacol. 1974 Jul 1;23(13):1910-3. doi: 10.1016/0006-2952(74)90201-9.
7
Oxygen radicals and hydrogen peroxide in rat brain mitochondria.大鼠脑线粒体中的氧自由基和过氧化氢
FEBS Lett. 1974 Sep 1;45(1):92-5. doi: 10.1016/0014-5793(74)80818-5.
8
NADPH-dependen lipid peroxidation catalyzed by purified NADPH-cytochrome C reductase from rat liver microsomes.由大鼠肝微粒体纯化的NADPH-细胞色素C还原酶催化的NADPH依赖性脂质过氧化作用。
Biochem Biophys Res Commun. 1972 Aug 21;48(4):789-95. doi: 10.1016/0006-291x(72)90676-6.
9
Evidence for superoxide generation by NADPH-cytochrome c reductase of rat liver microsomes.大鼠肝脏微粒体NADPH-细胞色素c还原酶产生超氧化物的证据。
Biochem Biophys Res Commun. 1972 Jun 9;47(5):1133-7. doi: 10.1016/0006-291x(72)90952-7.
10
A comparative study on the effects of phenobarbital and 3,4-benzpyrene on the hydroxylating enzyme system of rat-liver microsomes.苯巴比妥与3,4-苯并芘对大鼠肝脏微粒体羟化酶系统影响的比较研究。
Chem Biol Interact. 1969 Dec;1(2):125-37. doi: 10.1016/0009-2797(69)90001-5.

NADPH-细胞色素c还原酶对氧、人工受体及细胞色素P-450的还原作用之间的关系。

Relationship between the reduction of oxygen, artificial acceptors and cytochrome P-450 by NADPH--cytochrome c reductase.

作者信息

Lyakhovich V, Mishin V, Pokrovsky A

出版信息

Biochem J. 1977 Nov 15;168(2):133-9. doi: 10.1042/bj1680133.

DOI:10.1042/bj1680133
PMID:202259
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1183744/
Abstract

The interaction of NADPH--cytochrome c reductase with oxygen, artificial acceptors and cytochrome P-450 was studied. The generation of superoxide anion radicals (O2-.) from the oxidation of adrenaline to adrenochrome catalysed by NADPH--cytochrome c reductase proceeds independently of the interaction of the enzyme with the artificial anaerobic acceptors cytochrome c or 2,6-dichlorophenol-indophenol. Propyl 3,4,5-trihydroxybenzoate inhibited competitively the adrenaline oxidation by isolated NADPH--cytochrome c reductase (Ki 3.2--4.7 micrometer) and inhibited non-competitively the cytochrome c reduction (Ki 92--109 micrometer). In contrast with the process of electron transfer to cytochrome c, the rate of reduction of cytochrome P-450 and the rate of oxidation of adrenaline in liver microsomal fraction are correlated. Hexobarbital increases the Vmax. of adrenaline oxidation without affecting the Km value, whereas metyrapone, a metabolic inhibitor decreases Vmax. without affecting the Km. From the results obtained, some conclusions about NADPH--cytochrome c reductase function were made.

摘要

研究了NADPH-细胞色素c还原酶与氧气、人工受体及细胞色素P-450的相互作用。由NADPH-细胞色素c还原酶催化的肾上腺素氧化为肾上腺色素过程中超氧阴离子自由基(O2-·)的生成,独立于该酶与人工厌氧受体细胞色素c或2,6-二氯酚靛酚的相互作用。3,4,5-三羟基苯甲酸丙酯竞争性抑制分离的NADPH-细胞色素c还原酶对肾上腺素的氧化作用(抑制常数Ki为3.2-4.7微米),并非竞争性抑制细胞色素c的还原作用(抑制常数Ki为92-109微米)。与电子传递给细胞色素c的过程相反,肝脏微粒体部分中细胞色素P-450的还原速率与肾上腺素的氧化速率相关。己巴比妥增加肾上腺素氧化的最大反应速度(Vmax),而不影响米氏常数(Km)值;代谢抑制剂甲吡酮则降低Vmax,而不影响Km。根据所得结果,得出了一些关于NADPH-细胞色素c还原酶功能的结论。