A fully nonequilibrium concerted model for enzymes

✍ Scribed by J. S. Shiner

• Publisher: Wiley (John Wiley & Sons)
• Year: 1982
• Tongue: English
• Weight: 586 KB
• Volume: 21
• Category: Article
• ISSN: 0006-3525
• DOI: 10.1002/bip.360211111

✦ Synopsis

Abstract

The concerted model of Monod, Wyman, and Changeux is generalized so that all effects of interactions for an enzyme operating at a nonequilibrium stationary state are considered. In contrast to the original model, which is based on an analogy to equilibrium ligand binding, the generalization may show both “positive” and “negative cooperativity” in both catalytic binding and conformational processes. Furthermore, in contrast to any equilibrium binding model, the Hill coefficients may be greater than the number of sites n. For catalysis, the maximum value is 2__n__, and for conformational changes, n + 1. These points are illustrated by two cases that yield simpler analytic expressions. The first obtains when catalysis occurs on a much faster time scale than the conformational changes, and the second, when this situation is reversed.