The isolated iron-molybdenum cofactor of nitrogenase binds carbon monoxide upon electrochemically accessing reduced states

被引：24

作者：

Ibrahim, SK

Vincent, K

Gormal, CA

Smith, BE

Best, SP

Pickett, CJ

机构：

[1] John Innes Ctr, Nitrogen Fixat Lab, Norwich NR4 7UH, Norfolk, England

[2] Univ Melbourne, Sch Chem, Parkville, Vic 3052, Australia

来源：

CHEMICAL COMMUNICATIONS | 1999年 / 11期

关键词：

D O I：

10.1039/a902371b

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

The first spectroscopic evidence for the binding of a small gaseous molecule to the isolated iron molybdenum cofactor of nitrogenase (FeMoco) is presented: FTIR spectroelectrochemistry in a thin-layer cell shows that reduced FeMoco binds carbon monoxide and gives rise to v(CO) stretches that are close to those observed during turnover of the enzyme.

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页码：1019 / 1020

页数：2

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