Potentiometric titrations of carbon monoxide dehydrogenase and properties of the Ni-labile and nonlabile forms of the acetyl-COA synthase active site /

Carbon monoxide dehydrogenase (CODH) from Clostridium thermoaceticum is a bifunctional metalloenzyme, catalyzing the synthesis of acetyl-coenzyme A and reversible oxidation of CO to C02 at two novel Ni-Fe-S active sites (the A and C S,]2111, clusters, respectively). CODH also contains an [Fe, cube,...

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Bibliographic Details

Main Author:	Russell, William Kent
Format:	Thesis Book
Language:	English
Published:	[Place of publication not identified] : [publisher not identified] ; 1998.
Subjects:	Major chemistry.
Online Access:	http://proxy.library.tamu.edu/login?url=http://proquest.umi.com/pqdweb?did=737708951&sid=1&Fmt=2&clientId=2945&RQT=309&VName=PQD