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Intramolecularity and enzyme modelling: a critique

Sosale, Chandrasekhar (2003) Intramolecularity and enzyme modelling: a critique. In: Research on Chemical Intermediates, 29 (1). pp. 107-123.

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Official URL: http://www.springerlink.com/content/adk5w8g7eme92h...

Abstract

A critical reappraisal of the concept of intramolecularity is attempted, but particulary focussed on the effective molarity (EM) criterion and the relationship of intramolecularity to enzymic reactivity. The prevalent ambiguities in the EM concept are addressed and a revised definition (EM,v) is suggested. It is argued that there are fundamental limitations to the use of intramolecular reactions as enzyme models. Although the simplest mechanism for enzymic reactivity is based on transition state stabilisation, an alternative (although complex) possibility is based on the stabilisation of the enzyme. Possible mechanisms for the utilisation of the enzymic free energy for effecting catalysis are discussed.

Item Type: Journal Article
Additional Information: Copyright of this article belongs to Springer.
Keywords: catalysis;effective molarity;enzyme mechanism; enzyme-modelling;enzyme-stabilisation;intramolecularity;free energy;Michaelis-Menten;proximity.
Department/Centre: Division of Chemical Sciences > Organic Chemistry
Date Deposited: 26 Aug 2009 18:14
Last Modified: 26 Aug 2009 18:14
URI: http://eprints.iisc.ernet.in/id/eprint/17604

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