Consequences of removal of a molybdenum ligand (DmsA-Ser-176) of Escherichia coli dimethyl sulfoxide reductase.

Trieber, C A; Rothery, R A; Weiner, J H

Trieber, C A; Rothery, R A; Weiner, J H.

Affiliation

Trieber CA; Department of Biochemistry and the Medical Research Council Group in the Molecular Biology of Membranes, University of Alberta, Edmonton, Alberta T6G 2H7, Canada. joel.weiner@ualberta.ca

J Biol Chem ; 271(44): 27339-45, 1996 Nov 01.

Article in En | MEDLINE | ID: mdl-8910310

Subject(s)

Escherichia coli/enzymology; Iron-Sulfur Proteins; Molybdenum/metabolism; Oxidoreductases/chemistry; Oxidoreductases/metabolism; Protein Conformation; Amino Acid Sequence; Binding Sites; Electron Spin Resonance Spectroscopy; Kinetics; Molecular Sequence Data; Mutagenesis, Site-Directed; Recombinant Proteins/chemistry; Recombinant Proteins/metabolism; Sequence Homology, Amino Acid; Serine

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Collection: 01-internacional Database: MEDLINE Main subject: Oxidoreductases / Protein Conformation / Escherichia coli / Iron-Sulfur Proteins / Molybdenum Language: En Journal: J Biol Chem Year: 1996 Document type: Article Affiliation country: Canada

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