Volume changes during enzyme reactions: indications of enzyme pulsation during fumarase catalysis.

Abstract:

:Overall activation volumes for multistep reactions are not usually pressure independent. The present investigation gives a quantitative description of this effect under Theory. Simple relations are obtained which can easily be applied to experimental data and which allow more insight into the dynamics of enzyme reactions. This is demonstrated under Experimental Application for the conversion of fumarate to L-malate catalyzed by the enzyme fumarase. The volume profile of this reaction indicates a pulsation of the enzyme molecule during catalysis. The appendix discusses the question whether Eyring's transition-state theory is an appropriate basis for investigations of this kind.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Butz P,Greulich KO,Ludwig H

doi

10.1021/bi00405a024

subject

Has Abstract

pub_date

1988-03-08 00:00:00

pages

1556-63

issue

5

eissn

0006-2960

issn

1520-4995

journal_volume

27

pub_type

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