Metmyoglobin/Fluoride: Effect of Distal Histidine Protonation on the Association and Dissociation Rate Constants
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics
Reference38 articles.
1. Kinetic study of the reaction between cytochrome c peroxidase and hydrogen peroxide. Dependence on pH and ionic strength
2. Histidine 52 is a critical residue for rapid formation of cytochrome c peroxidase compound I
3. Kinetic studies of fluoride binding by cytochrome c peroxidase
4. Kinetic and equilibrium studies of cyanide binding by cytochrome c peroxidase
5. The effect of ionic strength on the kinetics of fluoride binding to cytochrome c peroxidase
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2. Hemoglobin and myoglobin stabilization by heme-fluoride complexes;Polyhedron;2021-07
3. Molecular Dynamics Simulation and Kinetic Study of Fluoride Binding to V21C/V66C Myoglobin with a Cytoglobin-like Disulfide Bond;International Journal of Molecular Sciences;2020-04-04
4. Distinct roles of a tyrosine-associated hydrogen-bond network in fine-tuning the structure and function of heme proteins: two cases designed for myoglobin;Molecular BioSystems;2016
5. Binding of imidazole, 1-methylimidazole and 4-nitroimidazole to yeast cytochrome c peroxidase (CcP) and the distal histidine mutant, CcP(H52L);Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics;2015-08
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