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芘连接的血红素结构域细胞色素P450 BM3电极催化的双氧还原反应

Reduction of dioxygen catalyzed by pyrene-wired heme domain cytochrome P450 BM3 electrodes.

作者信息

Udit Andrew K, Hill Michael G, Bittner V Garrett, Arnold Frances H, Gray Harry B

机构信息

Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125, USA.

出版信息

J Am Chem Soc. 2004 Aug 25;126(33):10218-9. doi: 10.1021/ja0466560.

DOI:10.1021/ja0466560
PMID:15315414
Abstract

We have electronically wired the cytochrome P450 BM3 heme domain to a graphite electrode with the use of a pyrene-terminated tether. AFM images clearly reveal that pyrene-wired enzyme molecules are adsorbed to the electrode surface. The enzyme-electrode system undergoes rapid and reversible electron transfer, displaying a standard rate constant higher than that of any other P450-electrode system. We also show that the graphite-pyrene-BM3 system catalyzes the four-electron reduction of dioxygen to water.

摘要

我们使用芘封端的连接链将细胞色素P450 BM3血红素结构域电连接到石墨电极上。原子力显微镜图像清楚地显示,芘连接的酶分子吸附在电极表面。该酶-电极系统经历快速且可逆的电子转移,其标准速率常数高于任何其他P450-电极系统。我们还表明,石墨-芘-BM3系统催化氧气的四电子还原生成水。

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