Molecular mechanism of myoglobin autoxidation: insights from computer simulations.

doi:10.1021/jp5093948

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Article

Molecular mechanism of myoglobin autoxidation: insights from computer simulations.

The journal of physical chemistry. B - 5 Feb 2015

Arcon J P, Rosi P, Petruk A A, Marti M A, Estrin D A

Abstract excerpt

Myoglobin (Mb) and hemoglobin have the biological ability to carry/store oxygen (O2), a property which requires its heme iron atom to be in the ferrous--Fe(II)--state. However, the thermodynamically stable state in the presence of O2 is Fe(III) and thus the oxidation rate of a globin is a critical parameter related to its function. Mb has been extensively studied and many mutants have been characterized regarding...

Topics

Catalysis
Computer Simulation
Heme
Hydrogen Bonding
Molecular Dynamics Simulation
Mutation
Myoglobin
Oxidation-Reduction
Oxygen
Quantum Theory
Thermodynamics

Source

Open in PubMed

Identifiers

PMID: 25578484
DOI: 10.1021/jp5093948

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 31 Aug 2026.

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