Tri-n-butyltin binding to a low-affinity site decreases the F 1F O-ATPase sensitivity to oligomycin in mussel mitochondria

Applied Organometallic Chemistry

Volumn 26, Issue 11, 2012, Pages 593-599

  Nesci, Salvatore ^a   Ventrella, Vittoria ^a   Trombetti, Fabiana ^a   Pirini, Maurizio ^a   Pagliarani, Alessandra ^a  

^a UNIVERSITY OF BOLOGNA   (Italy)

Author keywords

F 1F O ATPase; mitochondria; mussel; oligomycin sensitivity; tri n butyltin

Indexed keywords

ATP-ASE ACTIVITY; CATALYTIC FUNCTIONS; COVALENT BINDING; DIGESTIVE GLANDS; ENVIRONMENTAL POLLUTANTS; ENZYME COMPLEXES; HIGH-AFFINITY SITES; MITOCHONDRIAL DAMAGE; MOLECULAR MECHANISM; MUSSEL; OLIGOMYCIN; PROTON FLUX; RADICAL SPECIES; SUBMITOCHONDRIAL PARTICLES; SULFUR OXIDATION; TRI-N-BUTYLTIN;

CATALYSIS; MITOCHONDRIA; PROTONS; SHELLFISH; SULFUR;

ENZYME INHIBITION;

EID: 84867886088     PISSN: 02682605     EISSN: 10990739     Source Type: Journal    
DOI: 10.1002/aoc.2904     Document Type: Article

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