“Strange Kinetics” in the Temperature Dependence of Methionine Ligand Rebinding Dynamics in Cytochrome c
Author:
Affiliation:
1. Department of Chemistry, Boston University, Boston, Massachusetts 02215, United States
Publisher
American Chemical Society (ACS)
Subject
Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/jp400481m
Reference58 articles.
1. Role of Heme Iron Coordination and Protein Structure in the Dynamics and Geminate Rebinding of Nitric Oxide to the H93G Myoglobin Mutant
2. Determination of the Fe−CO Bond Energy in Myoglobin Using Heterodyne-Detected Transient Thermal Phase Grating Spectroscopy
3. Ligand Dynamics in an Electron Transfer Protein
4. Ultrafast dynamics of myoglobin probed by time-resolved resonance Raman spectroscopy
5. Microscopic model of carbon monoxide binding to myoglobin
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1. Adiabatic Ligand Binding in Heme Proteins: Ultrafast Kinetics of Methionine Rebinding in Ferrous Cytochrome c;The Journal of Physical Chemistry B;2018-09-19
2. Ultrafast CO Kinetics in Heme Proteins: Adiabatic Ligand Binding and Heavy Atom Tunneling;Journal of the American Chemical Society;2017-10-24
3. Quantum ergodicity and energy flow in molecules;Advances in Physics;2015-07-04
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