Proton TranslocatingATPases

Abstract

Originally published in: Handbook of ATPase. Edited by Masamitsu Futai, Yoh Wada and Jack H. Kaplan. Copyright © 2004 Wiley‐VCH Verlag GmbH & Co. KGaA Weinheim. Print ISBN: 3‐527‐30689‐3 The sections in this article are Introduction Catalytic Mechanism of F ‐ ATPase Roles of the γ subunit: energy coupling by mechanical rotation Roles of the γ Subunit in Energy Coupling γ Subunit Rotation Mutational Analysis of the γ Subunit Rotation Rotational Catalysis of the F ‐ ATPase Holoenzyme Structure of F o Sector and Proton Transport Pathway Rotational Catalysis of the F ‐ ATPase Holoenzyme Rotational Catalysis of F ‐ ATPase in Membranes Rotational catalysis of V ‐ ATPase Catalytic Site and Proton Pathway Subunit Rotation of V ‐ ATPase During Catalysis Conclusion Acknowledgments

Kinetic and hysteretic behavior of ATP hydrolysis of the highly stable dimeric ATP synthase of Polytomella sp.

“…Introduction 44 F-type ATPases are highly conserved oligomeric complexes that 45 play a central role in energy transduction in mitochondria, chloro- 46 plasts and bacterial membranes [1]. In particular, mitochondrial 47 F 1 F O -ATP synthase (H + -translocating adenosine triphosphatase, 48 EC 3.6.3.14) is a key participant in oxidative phosphorylation.…”