A scanning tunnelling study of immobilised cytochrome P450cam

被引：49

作者：

Davis, JJ ^{[1
]}

Djuricic, D ^{[1
]}

Lo, KKW ^{[1
]}

Wallace, ENK ^{[1
]}

Wong, LL ^{[1
]}

Hill, HAO ^{[1
]}

机构：

[1] Univ Oxford, Inorgan Chem Lab, Oxford OX1 3QR, England

来源：

FARADAY DISCUSSIONS | 2000年 / 116卷

关键词：

D O I：

10.1039/b001372m

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

A site-specifically engineered surface cysteine residue, located in a region where the haem moiety is closest to the surface, is used to anchor cytochrome P450(cam) enzyme molecules covalently to a gold electrode. More reproducibly ordered adsorption, at high coverage, occurs with this K344C mutant than with the wild-type enzyme. The subsequently formed close-packed monolayer arrays have been probed by scanning tunnelling microscopy under ambient conditions and under aqueous (buffered) solution at high resolution. Initial indications suggest that the immobilised enzyme is both electrochemically addressable and catalytically active.

引用

页码：15 / 22

页数：8

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