Catalytic sites of Escherichia coli F1-ATPase.
Catalytic sites of Escherichia coli F1-ATPase.
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大肠杆菌 F1-ATP 酶的催化位点。
DOI：
10.1007/bf00762365
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发表时间：
1992
影响因子：
3
通讯作者：
Senior,AE
中科院分区：
文献类型：
--
作者：
Senior,AE
对大肠杆菌F1-ATP酶催化位点的结构和功能进行了综述。结构预测、生化分析和诱变实验表明催化位点主要由 β 亚基的 137-335 残基形成。讨论了参与磷酸键裂解/合成和腺嘌呤环结合的位点的子结构域。讨论了由于催化位点协同性而导致稳态催化测量中固有的模糊性，并强调了前稳态（“单位点”）技术的优点。 F1-低聚物组装导致单个高亲和力催化位点的出现。描述了单位点催化速率和平衡常数的测量，以及通过不同的 pH、二甲基亚砜和突变对它们的调节，并提出了关于高亲和力催化位点的性质和催化机制的结论。
The catalytic site ofEscherichia coliF1-ATPase is reviewed in terms of structure and function. Structural prediction, biochemical analyses, and mutagenesis experiments suggest that the catalytic site is formed primarily by residues 137–335 of β-subunit. Subdomains of the site involved in phosphate-bond cleavage/synthesis and adenine-ring binding are discussed. Ambiguities inherent in steady-state catalytic measurements due to catalytic site cooperativity are discussed, and the advantages of pre-steady-state (“unisite”) techniques are emphasized. The emergence of a single high-affinity catalytic site occurs as a result of F1-oligomer assembly. Measurements of unisite catalysis rate and equilibrium constants, and their modulation by varied pH, dimethylsulfoxide, and mutations, are described and conclusions regarding the nature of the high-affinity catalytic site and mechanism of catalysis are presented.