Molecular Dynamics Simulation of Nitric Oxide in Myoglobin
Author:
Affiliation:
1. Department of Chemistry, University of Basel, Klingelbergstrasse 80, 4056 Basel, Switzerland
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/jp212112f
Reference76 articles.
1. The role of structure, energy landscape, dynamics, and allostery in the enzymatic function of myoglobin
2. FeNO Structure in Distal Pocket Mutants of Myoglobin Based on Resonance Raman Spectroscopy
3. Ultrafast relaxation in picosecond photolysis of nitrosylhemoglobin
4. Ligand binding and protein relaxation in heme proteins: a room temperature analysis of nitric oxide geminate recombination
5. Distal pocket residues affect picosecond ligand recombination in myoglobin. An experimental and molecular dynamics study of position 29 mutants.
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