Catalysis-enhancement via rotary fluctuation of F1-ATPase.

Abstract:

:Protein conformational fluctuations modulate the catalytic powers of enzymes. The frequency of conformational fluctuations may modulate the catalytic rate at individual reaction steps. In this study, we modulated the rotary fluctuation frequency of F1-ATPase (F1) by attaching probes with different viscous drag coefficients at the rotary shaft of F1. Individual rotation pauses of F1 between rotary steps correspond to the waiting state of a certain elementary reaction step of ATP hydrolysis. This allows us to investigate the impact of the frequency modulation of the rotary fluctuation on the rate of the individual reaction steps by measuring the duration of rotation pauses. Although phosphate release was significantly decelerated, the ATP-binding and hydrolysis steps were less sensitive or insensitive to the viscous drag coefficient of the probe. Brownian dynamics simulation based on a model similar to the Sumi-Marcus theory reproduced the experimental results, providing a theoretical framework for the role of rotational fluctuation in F1 rate enhancement.

journal_name

Biophys J

journal_title

Biophysical journal

authors

Watanabe R,Hayashi K,Ueno H,Noji H

doi

10.1016/j.bpj.2013.09.050

subject

Has Abstract

pub_date

2013-11-19 00:00:00

pages

2385-91

issue

10

eissn

0006-3495

issn

1542-0086

pii

S0006-3495(13)01127-2

journal_volume

105

pub_type

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