Chemical potential of bound ligand, an important parameter for free energy transduction
- 1 January 1981
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 78 (1) , 270-273
- https://doi.org/10.1073/pnas.78.1.270
Abstract
The chemical potential (.mu.L,b) of a ligand L bound to a protein or enzyme can be rigorously defined, and this paper describes some of its properties in relation to other thermodynamic parameters, with emphasis on thermodynamic parameters that may be used in the elucidation of the mechanism of biological free energy transduction. Free energy transduction involves the transfer of free energy from 1 molecule to another, and the actual transfer may often occur while both molecules are bound to the transducer enzyme, which means that .mu.L,b for 1 bound ligand increases at the expense of .mu.L,b for the other. The free energy change for the overall reaction may be very small, and it is not possible to express the phenomenon of transfer, in thermodynamic terms, without the explicit use of .mu.L,b as a parameter.This publication has 2 references indexed in Scilit:
- Glucose-induced conformational change in yeast hexokinase.Proceedings of the National Academy of Sciences, 1978
- Linked Functions and Reciprocal Effects in Hemoglobin: A Second LookAdvances in Protein Chemistry, 1964