ArticlePhysical chemistry chemical physics : PCCP2021
The redox potential of a heme cofactor in
Article in Physical chemistry chemical physics : PCCP, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 12 citations in OpenAlex.
- Toward Relative Redox Potential Predictions in Flavoproteins: Treatment of a Charge-Changing Mutation in Alchemical Free Energy Simulations.Journal of chemical theory and computation · 2026Article
- Excited States of Peridinin in PCP: A Polarizable Embedding QM/MM Study.The journal of physical chemistry. B · 2025Article
- How Aqueous Solvation Impacts the Frequencies and Intensities of Infrared Absorption Bands in Flavin: The Quest for a Suitable Solvent Model.Molecules (Basel, Switzerland) · 2024Article
- Structural Determinants of Redox Conduction Favor Robustness over Tunability in Microbial Cytochrome Nanowires.bioRxiv : the preprint server for biology · 2023Article
- Theoretical Modeling of Redox Potentials of Biomolecules.Molecules (Basel, Switzerland) · 2022Review
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Redox reactions are crucial to biological processes that protect organisms against oxidative stress. Metalloenzymes, such as peroxidases which reduce excess reactive oxygen species into water, play a key role in detoxification mechanisms. Here we present the results of a polarizable QM/MM study of the reduction potential of the electron transfer heme in the cytochrome c peroxidase of Nitrosomonas europaea. We have found that environment polarization does not substantially affect the computed value of the redox potential. Particular attention has been given to analyzing the role of electrostatic interactions within the protein environment and the solvent on tuning the redox potential of the heme co-factor. We have found that the electrostatic interactions predominantly explain the fluctuations of the vertical ionization/attachment energies of the heme for the sampled configurations, and that the long range electrostatic interactions (up to 40 Å) contribute substantially to the absolute values of the vertical energy gaps.
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Registered trials
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