Features of subunit NuoM (ND4) in Escherichia coli NDH-1: TOPOLOGY AND IMPLICATION OF CONSERVED GLU144 FOR COUPLING SITE 1.

Torres-Bacete, Jesus; Sinha, Prem Kumar; Castro-Guerrero, Norma; Matsuno-Yagi, Akemi; Yagi, Takao

Torres-Bacete, Jesus; Sinha, Prem Kumar; Castro-Guerrero, Norma; Matsuno-Yagi, Akemi; Yagi, Takao.

Affiliation

Torres-Bacete J; Department of Molecular and Experimental Medicine, The Scripps Research Institute, La Jolla, California 92037, USA.

J Biol Chem ; 284(48): 33062-9, 2009 Nov 27.

Article in En | MEDLINE | ID: mdl-19815558

Subject(s)

Escherichia coli Proteins/genetics; Glutamic Acid/genetics; Mutation; NADH Dehydrogenase/genetics; Binding Sites; Cell Membrane/enzymology; Escherichia coli/enzymology; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/metabolism; Glutamic Acid/metabolism; Immunoblotting; Membrane Proteins/chemistry; Membrane Proteins/genetics; Membrane Proteins/metabolism; Mutagenesis, Site-Directed; Mutant Proteins/chemistry; Mutant Proteins/metabolism; NADH Dehydrogenase/chemistry; NADH Dehydrogenase/metabolism; Protein Structure, Secondary; Protein Subunits/genetics; Protein Subunits/metabolism

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Glutamic Acid / Escherichia coli Proteins / Mutation / NADH Dehydrogenase Type of study: Prognostic_studies Language: En Journal: J Biol Chem Year: 2009 Document type: Article Affiliation country: United States

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