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催化过程中的亚基相互作用。线粒体腺苷三磷酸酶的交替位点协同性。

Subunit interaction during catalysis. Alternating site cooperativity of mitochondrial adenosine triphosphatase.

作者信息

Hutton R L, Boyer P D

出版信息

J Biol Chem. 1979 Oct 25;254(20):9990-3.

PMID:158596
Abstract

ATP concentration modulates oxygen exchange catalyzed by purified, soluble mitochondrial ATPase during ATP hydrolysis so that water oxygen incorporation into each Pi formed increases markedly as ATP concentration is lowered. This behavior is readily explained by catalytic cooperativity between subunits of the ATPase. However, other reasonable explanations also need consideration. A new approach for assessing these various explanations is used, based on measurement of the [18O]Pi species formed by hydrolysis of ATP highly labeled with 18O in the gamma-phosphoryl group. The results and other supporting data give what appears to be the most compelling evidence yet attained for alternating site catalytic cooperativity in an enzymic catalysis.

摘要

在ATP水解过程中，ATP浓度调节由纯化的可溶性线粒体ATP酶催化的氧交换，使得随着ATP浓度降低，形成的每个磷酸根中掺入的水氧显著增加。ATP酶亚基之间的催化协同作用很容易解释这种行为。然而，其他合理的解释也需要考虑。基于对γ-磷酸基团中用18O高度标记的ATP水解形成的[18O]磷酸根种类的测量，采用了一种评估这些不同解释的新方法。结果和其他支持数据给出了在酶催化中交替位点催化协同作用迄今最有说服力的证据。

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J Biol Chem. 1979 Oct 25;254(20):9990-3.
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