| Literature DB >> 2248999 |
Abstract
The electric charges on an enzyme may move concomitantly with a conformational change. Such an enzyme will absorb energy from an oscillating electric field. If in addition the enzyme has a larger association constant for substrate than for product, as is often true, it can use this energy to drive the catalyzed reaction away from equilibrium. Approximate analytical expressions are given for the field-driven flux, electrical power absorbed, free-energy produced per unit time, thermodynamic efficiency, and zero-flux concentrations. The field-driven flux is written as a generalized Michaelis-Menten equation.Mesh:
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Year: 1990 PMID: 2248999 PMCID: PMC1281042 DOI: 10.1016/S0006-3495(90)82441-3
Source DB: PubMed Journal: Biophys J ISSN: 0006-3495 Impact factor: 4.033