REACTIVITY OF RU-MODIFIED CYTOCHROME-C TOWARDS CYTOCHROME-OXIDASE AND CYTOCHROME REDUCTASE

被引：0
作者：
KAZMI, SA
机构：
来源：
JOURNAL OF THE CHEMICAL SOCIETY OF PAKISTAN | 1991年 / 13卷 / 01期
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O6 [化学];
学科分类号：
0703 ;
摘要：
Horse heart cytochrome c was reacted with aquopentaamine ruthenium(III). Ru pentaamine moiety attaches itself to His-33 of the protein molecule. Electron transfer reactivity of this Ru modified protein towards cytochrome-c reductase and cytochrome-c oxidase was measured and compared to the corresponding reactivities of the native protein. It was found that oxidase reaction of the modified protein, though similar in its ionic strength profile to the native protein, was moderately faster. For the reductase reaction, the Ru modified reaction was upto 2 orders of magnitude faster than the native protein. The acceleration depended upon ionic strength and pH. These results are interpreted to indicate that cytochrome-c has separate pathways for its reaction with oxidase and reductase.
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页码：49 / 53
页数：5
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