Activation of nit-1 nitrate reductase by W-formate dehydrogenase.

Abstract:

:Formate dehydrogenase ( FDH ) from Clostridium thermoaceticum is a known tungsten enzyme. FDH was tested for the presence of nitrogenase-type cofactor and nitrate reductase-type cofactor by the Azotobacter vinelandii UW-45 and Neurospora crassa nit-1 reconstitution assays, respectively. Tungsten formate dehydrogenase (W- FDH ), containing only a small Mo impurity, activated the nit-1 nitrate reductase extracts when molybdate was also added, but not when tungstate was added. These results show W- FDH contains the cofactor common to all known Mo-enzymes except nitrogenase. The difference between the redox chemistries of W- FDH and W-substituted sulfite oxidase appears to relate to differences in tungsten ligation other than that donated by the cofactor or to variations in the protein environment surrounding the tungsten active site.

authors

Deaton JC,Solomon EI,Durfor CN,Wetherbee PJ,Burgess BK,Jacobs DB

doi

10.1016/0006-291x(84)90782-4

subject

Has Abstract

pub_date

1984-06-29 00:00:00

pages

1042-7

issue

3

eissn

0006-291X

issn

1090-2104

pii

0006-291X(84)90782-4

journal_volume

121

pub_type

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