The Escherichia coli metal-binding chaperone SlyD interacts with the large subunit of [NiFe]-hydrogenase 3

FEBS Letters

Volumn 585, Issue 2, 2011, Pages 291-294

  Chan Chung, Kim C ^a   Zamble, Deborah B ^a  

^a UNIVERSITY OF TORONTO   (Canada)

Author keywords

NiFe Hydrogenase; Accessory protein interaction; Chaperones; Metal center assembly; Nickel; SlyD

Indexed keywords

BINDING PROTEIN; CHAPERONE; ENZYME VARIANT; IRON; NICKEL; NICKEL IRON HYDROGENASE; NICKEL IRON HYDROGENASE 3; PROTEIN HYPA; PROTEIN HYPB; PROTEIN SLYD; UNCLASSIFIED DRUG;

ARTICLE; BACTERIAL GROWTH; COMPLEX FORMATION; CONTROLLED STUDY; ENZYME ANALYSIS; ENZYME MODIFICATION; ENZYME SUBUNIT; ENZYME SYNTHESIS; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; PROTEIN ISOLATION; PROTEIN PROTEIN INTERACTION; WESTERN BLOTTING;

CARRIER PROTEINS; ESCHERICHIA COLI PROTEINS; GTP-BINDING PROTEINS; HYDROGENASE; METALS; MULTIPROTEIN COMPLEXES; PEPTIDYLPROLYL ISOMERASE; PROTEIN BINDING;

ESCHERICHIA COLI;

EID: 78651377686     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2010.12.024     Document Type: Article

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