Characterization of the catalytic and noncatalytic ADP binding sites of the F1-ATPase from the thermophilic bacterium, PS3.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
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1. Characteristics of protection by MgADP and MgATP of α3β3Γ subcomplex of thermophilic Bacillus PS3 βY341W-mutant F1-ATPase from inhibition by 7-chloro-4-nitrobenz-2-oxa-1,3-diazole support a Bi-site mechanism of catalysis;Biochemistry (Moscow);2011-11
2. A bi-site mechanism for Escherichia coli F1-ATPase accounts for the observed positive catalytic cooperativity;Biochimica et Biophysica Acta (BBA) - Bioenergetics;2009-08
3. Structure and Mechanism of F0F1-Type ATP Synthases and ATPases;Advances in Enzymology - and Related Areas of Molecular Biology;2006-11-22
4. The presence of phosphate at a catalytic site suppresses the formation of the MgADP-inhibited form of F1-ATPase;European Journal of Biochemistry;2002-01
5. The participation of metals in the mechanism of the F1-ATPase;Biochimica et Biophysica Acta (BBA) - Bioenergetics;2000-05
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