一氧化碳和氰化物与固氮酶的铁钼辅因子的协同结合：一种古老酶的残留化学特性？

Synergic binding of carbon monoxide and cyanide to the FeMo cofactor of nitrogenase: relic chemistry of an ancient enzyme?

作者信息

Pickett Christopher J, Vincent Kylie A, Ibrahim Saad K, Gormal Carol A, Smith Barry E, Fairhurst Shirley A, Best Stephen P

机构信息

Department of Biological Chemistry, John Innes Centre, Norwich NR4 7UH, UK.

出版信息

Chemistry. 2004 Oct 4;10(19):4770-6. doi: 10.1002/chem.200400382.

DOI:10.1002/chem.200400382

PMID:15372690

Abstract

The first electrochemical and infra-red data on the binding of cyanide to the isolated iron-molybdenum cofactor of nitrogenase, FeMoco, is described. It is shown that cyanide stabilises a hitherto unrecognised, low-spin, EPR-active (S= 1/2), superoxidised form of FeMoco, and we provide the first evidence that carbon monoxide and cyanide bind synergically to the oxidised and semireduced states of the isolated cofactor, states which are unreactive to carbon monoxide alone.

摘要

本文描述了关于氰化物与固氮酶的分离铁钼辅因子（FeMoco）结合的首批电化学和红外数据。结果表明，氰化物能稳定一种迄今未被识别的、低自旋、具有电子顺磁共振活性（S = 1/2）的FeMoco超氧化形式，并且我们首次提供证据表明一氧化碳和氰化物能协同结合到分离辅因子的氧化态和半还原态，而这些状态单独对一氧化碳无反应。