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Volume 271, Number 24, Issue of June 14, 1996 pp. 14256-14263
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

Carbon Monoxide Dehydrogenase from Methanosarcina frisia Gö1
CHARACTERIZATION OF THE ENZYME AND THE REGULATED EXPRESSION OF TWO OPERON-LIKE cdh GENE CLUSTERS

(Received for publication, December 5, 1995, and in revised form, February 28, 1996)

Rik I. L. Eggen Dagger , Richard van Kranenburg Dagger , Aldwin J. M. Vriesema Dagger , Ans C. M. Geerling Dagger , Mark F. J. M. Verhagen , Wilfred R. Hagen and Willem M. de Vos Dagger

From the Departments of Dagger  Microbiology and  Biochemistry, Wageningen Agricultural University, Wageningen 6703 CT, The Netherlands

Carbon monoxide dehydrogenase (Cdh) has been anaerobically purified from Methanosarcina frisia Gö1. The enzyme is a Ni2+-, Fe2+-, and S2--containing alpha 2beta 2 heterotetramer of 214 kDa with a pI of 5.2 and subunits of 94 and 19 kDa. It has a Vmax of 0.3 mmol of CO min-1 mg-1 and Km values for CO and methyl viologen of approx 0.9 mM and 0.12 mM, respectively. EPR spectroscopy on the reduced enzyme showed two overlapping signals: one indicative for 2 (4Fe-4S)+ clusters and a second signal that is atypical for standard Fe/S clusters. The latter was, together with high-spin EPR signals of the oxidized enzyme tentatively assigned to an Fe/S cluster of high nuclearity.


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 Proc. Natl. Acad. Sci. USAHome page
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Copyright © 1996 by the American Society for Biochemistry and Molecular Biology.