Assessment of total catalytic sites and the nature of bound nucleotide participation in photophosphorylation.

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作者信息

Rosen G, Gresser M, Vinkler C, Boyer P D

出版信息

J Biol Chem. 1979 Nov 10;254(21):10654-61.

PMID:500602

Abstract

摘要

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Assessment of total catalytic sites and the nature of bound nucleotide participation in photophosphorylation.

J Biol Chem. 1979 Nov 10;254(21):10654-61.

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引用本文的文献

Evaluation by steady-state enzyme kinetics of the role of tightly bound nucleotides during photophosphorylation.通过稳态酶动力学评估紧密结合的核苷酸在光合磷酸化过程中的作用。

J Bioenerg Biomembr. 1983 Oct;15(5):257-76. doi: 10.1007/BF00744524.

Photoaffinity labeling with 2-azidoadenosine diphosphate of a tight nucleotide binding site on chloroplast coupling factor 1.用 2-叠氮腺苷二磷酸对叶绿体偶联因子 1 上的一个紧密核苷酸结合位点进行光亲和标记。

Proc Natl Acad Sci U S A. 1982 Dec;79(24):7744-8. doi: 10.1073/pnas.79.24.7744.

Substrate binding affinity changes in mitochondrial energy-linked reactions.线粒体能量偶联反应中底物结合亲和力的变化。

Proc Natl Acad Sci U S A. 1982 Mar;79(6):1756-60. doi: 10.1073/pnas.79.6.1756.

Conformational coupling in H+-pumps and ATP synthesis--its analysis with anisotropic inhibitors of energy transduction in oxidative phosphorylation.H⁺泵与ATP合成中的构象偶联——利用氧化磷酸化中能量转导的各向异性抑制剂进行分析

Mol Cell Biochem. 1984;61(1):37-61. doi: 10.1007/BF00239605.

The proton-ATPase of bacteria and mitochondria.细菌和线粒体的质子 - ATP酶。

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Energy coupling to ATP synthesis by the proton-translocating ATPase.质子转运ATP酶将能量与ATP合成相偶联。

J Membr Biol. 1982;67(1):1-12. doi: 10.1007/BF01868643.

Vacuolar ATPases, like F1,F0-ATPases, show a strong dependence of the reaction velocity on the binding of more than one ATP per enzyme.液泡ATP酶与F1、F0-ATP酶一样，其反应速度强烈依赖于每个酶结合不止一个ATP。

Proc Natl Acad Sci U S A. 1989 Nov;86(22):8708-11. doi: 10.1073/pnas.86.22.8708.

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