Rotating proton pumping ATPases: subunit/subunit interactions and thermodynamics.

Abstract:

:In this article, we discuss single molecule observation of rotational catalysis by E. coli ATP synthase (F-ATPase) using small gold beads. Studies involving a low viscous drag probe showed the stochastic properties of the enzyme in alternating catalytically active and inhibited states. The importance of subunit interaction between the rotor and the stator, and thermodynamics of the catalysis are also discussed. "Single Molecule Enzymology" is a new trend for understanding enzyme mechanisms in biochemistry and physiology.

journal_name

IUBMB Life

journal_title

IUBMB life

authors

Nakanishi-Matsui M,Sekiya M,Futai M

doi

10.1002/iub.1134

subject

Has Abstract

pub_date

2013-03-01 00:00:00

pages

247-54

issue

3

eissn

1521-6543

issn

1521-6551

journal_volume

65

pub_type

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