抗坏血酸还原单位点氧化还原蛋白的机制。
The mechanism of reduction of single-site redox proteins by ascorbic acid.
作者信息
Al-Ayash A I, Wilson M T
出版信息
Biochem J. 1979 Feb 1;177(2):641-8. doi: 10.1042/bj1770641.
Abstract
The reduction of single-site haem and copper redox proteins by ascorbic acid was studied as a function of pH. Evidence is presented that indicates that the double-deprotonated ascorbate anion, ascorbate2-, is the reducing agent, and the pH-independent second-order rate constants for reduction by this species are given. Investigation of the temperature dependences of these rate constants have yielded the values of the activation parameters (delta H++ and delta S++) for reduction. These values, together with ligand-replacement studies, suggest that ascorbate2- acts as an outer-sphere reductant for these proteins. Reasons to account for the apparent inability of ascorbic acid to reduce the alkaline conformer of mammalian ferricytochrome c are suggested.
摘要
研究了抗坏血酸对单一位点血红素和铜氧化还原蛋白的还原作用与pH值的关系。有证据表明，双去质子化的抗坏血酸阴离子（抗坏血酸根离子2-）是还原剂，并给出了该物种还原反应的与pH无关的二级速率常数。对这些速率常数的温度依赖性进行研究，得出了还原反应的活化参数（ΔH++和ΔS++）值。这些值与配体置换研究一起表明，抗坏血酸根离子2-作为这些蛋白质的外层球型还原剂。提出了一些理由来解释抗坏血酸明显无法还原哺乳动物高铁细胞色素c的碱性构象的原因。
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