The β subunit loop that couples catalysis and rotation in ATP synthase has a critical length

Journal of Biological Chemistry

Volumn 286, Issue 34, 2011, Pages 29788-29796

  Mnatsakanyan, Nelli ^a,b   Kemboi, Silas K ^a,b   Salas, Jasmin ^a,b   Weber, Joachim ^a,b  

^a TEXAS TECH UNIVERSITY   (United States)

^b TEXAS TECH UNIVERSITY HEALTH SCIENCES CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ATP SYNTHASE; ATP SYNTHESIS; C-TERMINAL DOMAINS; CATALYTIC SITES; CHARGED RESIDUES; CHEMICAL ENERGY; CRITICAL LENGTH; DELETION MUTANTS; ENZYMATIC ACTIVITIES; FLUORESCENCE RESONANCE ENERGY TRANSFER; HIGH-AFFINITY SITES; MECHANICAL ENERGIES; MODELING RESULTS; NEGATIVE CHARGE;

AMINO ACIDS; BACTERIOLOGY; BINDING SITES; CATALYSIS; ENERGY TRANSFER; FLUORESCENCE; ROTATION;

BINDING ENERGY;

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; ADENOSINE TRIPHOSPHATE MAGNESIUM; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE;

ARTICLE; BACILLUS; BETA CHAIN; BINDING AFFINITY; CATALYSIS; CONTROLLED STUDY; ENZYME ACTIVITY; FLUORESCENCE RESONANCE ENERGY TRANSFER; NONHUMAN; OXIDATIVE PHOSPHORYLATION; POINT MUTATION; PRIORITY JOURNAL; PROTEIN MOTIF;

ADENOSINE TRIPHOSPHATE; AMINO ACID MOTIFS; ATP SYNTHETASE COMPLEXES; BACILLUS; BACTERIAL PROTEINS; CATALYSIS; CATALYTIC DOMAIN; FLUORESCENCE RESONANCE ENERGY TRANSFER; MUTATION; PROTEIN SUBUNITS;

EID: 80051936240     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.254730     Document Type: Article

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