Inactivation of acetyl-CoA synthase/carbon monoxide dehydrogenase by copper

被引:58
作者
Bramlett, MR
Tan, XS
Lindahl, PA [1 ]
机构
[1] Texas A&M Univ, Dept Biochem & Biophys, College Stn, TX 77843 USA
[2] Texas A&M Univ, Dept Chem, College Stn, TX 77843 USA
关键词
D O I
10.1021/ja0352855
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Two recent crystal structures of acetyl-CoA synthase (ACS) from Moorella thermoacetica exhibited different metal contents and geometries at their active site, called the A-cluster. This led to the proposal of two catalytic mechanisms, one Ni-based, the other Cu-based. ACS was studied with respect to synthase activity, methyl group transfer activity, metal content, and EPR spectroscopy. Our results indicate that Cu is not required for catalysis and that it inactivates ACS by binding to the proximal site of the A-cluster. With Cu in this site, the A-cluster cannot accept a methyl group from the corrinoid-iron-sulfur protein, nor can it exhibit the NiFeC EPR signal after treatment with CO. Copyright © 2003 American Chemical Society.
引用
收藏
页码:9316 / 9317
页数:2
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