[2Fe-2S]-Ferredoxin binds directly to cysteine desulfurase and supplies an electron for iron-sulfur cluster assembly but is displaced by the scaffold protein or bacterial frataxin

Journal of the American Chemical Society

Volumn 135, Issue 22, 2013, Pages 8117-8120

  Kim, Jin Hae ^a   Frederick, Ronnie O ^a   Reinen, Nichole M ^a   Troupis, Andrew T ^a   Markley, John L ^a  

^a UNIVERSITY OF WISCONSIN MADISON   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE DESULFURASE; DISULFIDE BRIDGE; ENZYMATIC CONVERSIONS; EXPERIMENTAL EVIDENCE; IRON-SULFUR CLUSTERS; MUTUAL EXCLUSIONS; OXIDIZING AGENTS; SCAFFOLD PROTEIN;

AMINO ACIDS; BIOSYNTHESIS; COVALENT BONDS; ELECTRONS; ESCHERICHIA COLI; PROTEINS; SCAFFOLDS (BIOLOGY); SULFUR;

IRON COMPOUNDS;

ALANINE; CYSTATHIONINE GAMMA LYASE; CYSTEINE; FERREDOXIN; FRATAXIN; IRON; SCAFFOLD PROTEIN; SULFUR;

ARTICLE; BINDING AFFINITY; BINDING SITE; BIOGENESIS; CHEMICAL PARAMETERS; CONTROLLED STUDY; ELECTRON; ENZYME CONVERSION; INHIBITION KINETICS; MOLECULAR INTERACTION; MOLECULAR MECHANICS; NONHUMAN; OPERON; OXIDATION;

BINDING SITES; CARBON-SULFUR LYASES; CRYSTALLOGRAPHY, X-RAY; ELECTRONS; ESCHERICHIA COLI; FERREDOXINS; IRON; IRON-BINDING PROTEINS; MODELS, MOLECULAR; SULFUR;

EID: 84878638881     PISSN: 00027863     EISSN: 15205126     Source Type: Journal    
DOI: 10.1021/ja401950a     Document Type: Article

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