过氧化氢形成并还原细胞色素c氧化酶的“过氧”中间体
Formation and reduction of a 'peroxy' intermediate of cytochrome c oxidase by hydrogen peroxide.
作者信息
Wrigglesworth J M
出版信息
Biochem J. 1984 Feb 1;217(3):715-9. doi: 10.1042/bj2170715.
Abstract
In the presence of micromolar concentrations of H2O2, ferric cytochrome c oxidase forms a stable complex characterized by an increased absorption intensity at 606-607 nm with a weaker absorption band in the 560-580 nm region. Higher (millimolar) concentrations of H2O2 result in an enzyme exhibiting a Soret band at 427 nm and an alpha-band of increased intensity in the 589-610 nm region. Addition of H2O2 to ferric cytochrome c oxidase in the presence of cyanide results in absorbance increases at 444nm and 605nm. These changes are not seen if H2O2 is added to the cyanide complex of the ferric enzyme. The results support the idea that direct reaction of H2O2 with ferric cytochrome a 3 produces a 'peroxy' intermediate that is susceptible to further reduction by H2O2 at higher peroxide concentrations. Electron flow through cytochrome a is not involved, and the final product of the reaction is the so-called 'pulsed' or 'oxygenated' ferric form of the enzyme.
摘要
在微摩尔浓度的过氧化氢存在下，高铁细胞色素c氧化酶形成一种稳定的复合物，其特征是在606 - 607 nm处吸收强度增加，在560 - 580 nm区域有较弱的吸收带。较高（毫摩尔）浓度的过氧化氢会导致该酶在427 nm处呈现索雷特带，在589 - 610 nm区域α带强度增加。在氰化物存在下，向高铁细胞色素c氧化酶中添加过氧化氢会导致在444 nm和605 nm处吸光度增加。如果将过氧化氢添加到高铁酶的氰化物复合物中，则不会出现这些变化。这些结果支持这样一种观点，即过氧化氢与高铁细胞色素a3的直接反应产生一种“过氧”中间体，在较高的过氧化物浓度下，该中间体易于被过氧化氢进一步还原。电子通过细胞色素a的流动不参与其中，反应的最终产物是该酶所谓的“脉冲式”或“氧化态”高铁形式。
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