细胞色素c的氧化态依赖性ATP结合位点。一种可能的生理意义。
The oxidation-state-dependent ATP-binding site of cytochrome c. A possible physiological significance.
作者信息
Corthésy B E, Wallace C J
出版信息
Biochem J. 1986 Jun 1;236(2):359-64. doi: 10.1042/bj2360359.
Abstract
Cytochrome c binds certain physiological anions that are known to modulate the biological properties of the protein, although it is not known whether this effect is fortuitous or has physiological significance. We have examined the ability of the protein and its semisynthetic analogues to associate with certain of these anions, e.g. ATP, ADP, Pi and citrate. Our results show that specific residues or clusters of residues on the surface of horse heart cytochrome c are involved in the recognition sites for these anions. We also observed that binding at one site is linked to the oxidation state of the protein.
摘要
细胞色素c能结合某些已知可调节该蛋白质生物学特性的生理阴离子，尽管尚不清楚这种作用是偶然的还是具有生理意义。我们已经研究了该蛋白质及其半合成类似物与其中某些阴离子（例如ATP、ADP、磷酸根离子和柠檬酸根离子）结合的能力。我们的结果表明，马心细胞色素c表面的特定残基或残基簇参与了这些阴离子的识别位点。我们还观察到，在一个位点的结合与该蛋白质的氧化态有关。
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本文引用的文献
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