Kinetics of hemoglobin and transition state theory.
Open Access
- 1 May 1978
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 75 (5), 2108-2111
- https://doi.org/10.1073/pnas.75.5.2108
Abstract
Experimental evidence indicates that the way cooperativity in Hb is manifested kinetically depends on the nature of the ligand. The qualitative differences in the kinetics of NO, O2, CO and bulky isocyanides can be understood in structural terms in a framework based on transition state theory.This publication has 23 references indexed in Scilit:
- Structure and function of haemoglobinProgress in Biophysics and Molecular Biology, 1976
- Structure of horse carbonmonoxyhaemoglobinJournal of Molecular Biology, 1976
- Nitrosylmetalloporphyrins. III. Synthesis and molecular stereochemistry of nitrosyl-.alpha.,.beta.,.gamma.,.delta.-tetraphenylporphinato(1-methylimidazole)iron(II)Journal of the American Chemical Society, 1976
- Influence of globin structures on the state of the heme. IV. Ferrous low spin derivativesBiochemistry, 1976
- Dynamics of ligand binding to myoglobinBiochemistry, 1975
- Neutron Diffraction Analysis of Myoglobin: Structure of the Carbon Monoxide DerivativeScience, 1975
- Conformation, co-operativity and ligand binding in human hemoglobinJournal of Molecular Biology, 1975
- Studies on the reaction of isocyanides with haemproteins: I. Equilibria and kinetics of the binding to the isolated chains of human haemoglobinJournal of Molecular Biology, 1971
- Stereochemistry of Cooperative Effects in Haemoglobin: Haem–Haem Interaction and the Problem of AllosteryNature, 1970
- Parameters for the Description of Transition StatesScience, 1953