Complex cooperativity of ATP hydrolysis in the F1-ATPase molecular motor

✍ Scribed by Ming S. Liu; B.D. Todd; Richard J. Sadus

• Publisher: Elsevier Science
• Year: 2004
• Tongue: English
• Weight: 278 KB
• Volume: 1698
• Category: Article
• ISSN: 1570-9639
• DOI: 10.1016/j.bbapap.2003.11.033

✦ Synopsis

F 1 -ATPase catalyses ATP hydrolysis and converts the cellular chemical energy into mechanical rotation. The hydrolysis reaction in F 1 -ATPase does not follow the widely believed Michaelis -Menten mechanism. Instead, the hydrolysis mechanism behaves in an ATPdependent manner. We develop a model for enzyme kinetics and hydrolysis cooperativity of F 1 -ATPase which involves the binding-state changes to the coupling catalytic reactions. The quantitative analysis and modeling suggest the existence of complex cooperative hydrolysis between three different catalysis sites of F 1 -ATPase. This complexity may be taken into account to resolve the arguments on the binding change mechanism in F 1 -ATPase.