PMID: 1121Oct 1, 1975

Hypothesis on the role of liganded states of proteins in energy transducing systems

Bio Systems
A Bennun


In energy transducing systems the direction of energy transfer is proposed to be maintained by the synchronized turnovers of the conformational change of one protein coupling up to affect another. Catalysis by those systems implies, therefore, that under new space restrictions the groups of the transducing enzyme increase and decrease reactivity between themselves, with activatory and/or inhibitory ligands (H+, H2O, metals, etc.) and with the electron shells of the reactant molecules. The exergonic reaction-dependent turnover of the forms of the enzyme within the transition complexes would be maintained, therefore, under asymmetric phase angles of conformational-dependent reactivity that would effectively restrict the microscopic reversibility of transducing systems. Some well known reactions, such as hemoglobins Bohr effect, can be used to illustrate that microscopic (molecular) interactions subject to thermodynamic equilibria laws may similarly paricipate as driving forces in energy transducing sytems. This would allow the thermodynamic description of the role of proton translocation as that of a modificatory force of the structural parameters of proteins. Similarly, the relationship between the liganded states of hemoglobin ...Continue Reading


Feb 18, 1974·Annals of the New York Academy of Sciences·R E Dickerson


Dec 1, 1981·Journal of Bioenergetics and Biomembranes·H OhanianA Bennun
Dec 10, 1976·Molecular and Cellular Biochemistry·R Harris, A Bennun
Jul 1, 1994·Molecular Reproduction and Development·S VijayaraghavanK Hermsmeyer

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