Mössbauer and EPR Study of the Ni-Activated α-Subunit of Carbon Monoxide Dehydrogenase from Clostridium thermoaceticum

The A-center of carbon monoxide dehydrogenase (CODH) resides in the enzyme's α-subunit and is responsible for the acetyl-CoA synthase activity. The center comprises a Ni site and an iron−sulfur cluster. We have isolated the α-subunit using both continuous and discontinuous electrophoresis metho...

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Bibliographic Details
Published in:Journal of the American Chemical Society 1997-09, Vol.119 (35), p.8301-8312
Main Authors: Xia, Jinqiang, Hu, Zhengguo, Popescu, Codrina V, Lindahl, Paul A, Münck, Eckard
Format: Article
Language:English
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Summary:The A-center of carbon monoxide dehydrogenase (CODH) resides in the enzyme's α-subunit and is responsible for the acetyl-CoA synthase activity. The center comprises a Ni site and an iron−sulfur cluster. We have isolated the α-subunit using both continuous and discontinuous electrophoresis methods. When incubated with CO, samples prepared using continuous gels attain the Ared-CO state that exhibits an S = 1/2 EPR feature (g = 2.048, 2.046, 2.021) similar to the so-called NiFeC signal of native CODH. Both signals consistently quantify to
ISSN:0002-7863
1520-5126
DOI:10.1021/ja971025+