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Rate constants and equilibrium constants for the elementary steps of ATP hydrolysis by beef heart mitochondrial ATPase.

作者信息

Penefsky H S

出版信息

Methods Enzymol. 1986;126:608-18. doi: 10.1016/s0076-6879(86)26064-4.

DOI:10.1016/s0076-6879(86)26064-4
PMID:2908471
Abstract
摘要

相似文献

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Rate constants and equilibrium constants for the elementary steps of ATP hydrolysis by beef heart mitochondrial ATPase.牛肉心线粒体ATP酶催化ATP水解各基元步骤的速率常数和平衡常数。
Methods Enzymol. 1986;126:608-18. doi: 10.1016/s0076-6879(86)26064-4.
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Mechanism of ATP hydrolysis by beef heart mitochondrial ATPase. Rate constants for elementary steps in catalysis at a single site.牛心线粒体ATP酶催化ATP水解的机制。单个位点催化基本步骤的速率常数。
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On the rate of F1-ATPase turnover during ATP hydrolysis by the single catalytic site. Evidence that hydrolysis with a slow rate of product release does not occur at the alternating active site.
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Mechanism of ATP hydrolysis by beef heart mitochondrial ATPase. Rate enhancements resulting from cooperative interactions between multiple catalytic sites.牛肉心线粒体ATP酶催化ATP水解的机制。多个催化位点之间协同相互作用导致的速率增强。
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Mechanism of ATP synthesis by mitochondrial ATP synthase from beef heart.来自牛心线粒体ATP合酶合成ATP的机制。
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The complex of mitochondrial F1-ATPase with the natural inhibitor protein is unable to catalyze single-site ATP hydrolysis.线粒体F1 - ATP合酶与天然抑制蛋白形成的复合物无法催化单一位点的ATP水解。
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Relevance of divalent cations to ATP-driven proton pumping in beef heart mitochondrial F0F1-ATPase.二价阳离子与牛肉心线粒体F0F1 - ATP酶中ATP驱动的质子泵浦的相关性
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Mechanism and regulation of mitochondrial ATP synthesis.
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Aurovertin binding sites on beef heart mitochondrial F1-ATPase. Study with [14C]aurovertin D of the binding stoichiometry and of the interaction between aurovertin and the natural ATPase inhibitor for binding to F1.牛心线粒体F1-ATP酶上金褐霉素的结合位点。用[14C]金褐霉素D研究其结合化学计量以及金褐霉素与天然ATP酶抑制剂之间与F1结合的相互作用。
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