Catalytic site occupancy during ATP synthase catalysis
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Reference29 articles.
1. Evidence that energization of the chloroplast ATP synthase favors ATP formation at the tight binding catalytic site and increases the affinity for ADP at another catalytic site.
2. The binding change mechanism for ATP synthase — Some probabilities and possibilities
3. Specific placement of tryptophan in the catalytic sites of Escherichia coli F1-ATPase provides a direct probe of nucleotide binding: maximal ATP hydrolysis occurs with three sites occupied.
4. Specific Tryptophan Substitution in Catalytic Sites of Escherichia coli F1-ATPase Allows Differentiation between Bound Substrate ATP and Product ADP in Steady-state Catalysis
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