Involvement of ATP synthase residues αArg-376, βArg-182, and βLys-155 in Pi binding

FEBS Letters

Volumn 579, Issue 2, 2005, Pages 523-528

  Ahmad, Zulfiqar ^a   Senior, Alan E ^a  

^a UNIVERSITY OF ROCHESTER MEDICAL CENTER   (United States)

Author keywords

ATP synthase; ATP synthesis mechanism; Catalytic site E; Oxidative phosphorylation; Pi binding residue

Indexed keywords

4 CHLORO 7 NITROBENZOFURAZAN; ADENOSINE TRIPHOSPHATASE; ARGININE; LYSINE; PROTEINASE INHIBITOR; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE;

ARTICLE; CHEMICAL REACTION; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME PURIFICATION; ENZYME SUBSTRATE; ESCHERICHIA COLI; GENE MUTATION; NONHUMAN; NUCLEOTIDE METABOLISM; PRIORITY JOURNAL; PROTECTION; WILD TYPE;

4-CHLORO-7-NITROBENZOFURAZAN; ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; ARGININE; BACTERIAL PROTON-TRANSLOCATING ATPASES; BINDING SITES; CATALYTIC DOMAIN; ESCHERICHIA COLI; LYSINE; POINT MUTATION; SUBSTRATE SPECIFICITY;

ESCHERICHIA COLI;

EID: 11844258832     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2004.12.022     Document Type: Article

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