细胞色素c氧化酶反应中顺磁性氧中间体的结构。
The structure of the paramagnetic oxygen intermediate in the cytochrome c oxidase reaction.
作者信息
Hansson O, Karlsson B, Aasa R, Vänngård T, Malmström B G
出版信息
EMBO J. 1982;1(11):1295-7. doi: 10.1002/j.1460-2075.1982.tb01313.x.
Abstract
A paramagnetic intermediate with an unusual e.p.r. spectrum is formed when fully reduced cytochrome c oxidase is allowed to react with dioxygen at 173 K. The effect on the e.p.r. spectrum of using dioxygen enriched in 17O was investigated. These experiments show that an oxygen atom derived from dioxygen is bound to Cu2+ in the intermediate. The e.p.r. parameters can be explained in terms of a weak antiferromagnetic interaction (J approximately equal to 10 cm-1) between Cu2+B and cytochrome a3 in the low-spin ferryl ion state. It is suggested that an OH- ion bound to Cu2+B is hydrogen bonded to the oxygen atom of the ferryl ion in cytochrome a3.
摘要
当完全还原的细胞色素c氧化酶在173 K与双氧反应时，会形成一种具有异常电子顺磁共振（e.p.r.）光谱的顺磁性中间体。研究了使用富含17O的双氧对e.p.r.光谱的影响。这些实验表明，双氧衍生的一个氧原子与中间体中的Cu2+结合。e.p.r.参数可以用低自旋高铁离子状态下Cu2+B和细胞色素a3之间的弱反铁磁相互作用（J约等于10 cm-1）来解释。有人提出，与Cu2+B结合的OH-离子通过氢键与细胞色素a3中铁离子的氧原子相连。
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