ArticleScientific reports2016
Polarizability of the active site of cytochrome c reduces the activation barrier for electron transfer.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Article
- Neurovascular Signaling at the Gliovascular Interface: From Flow Regulation to Cognitive Energy Coupling.International journal of molecular sciences · 2025Review
- The Effect of Electron Spin-Dependent Polarizability on Protein Activity.Biomolecules · 2025Review
- Cytochrome "nanowires" are physically limited to sub-picoamp currents that suffice for cellular respiration.Frontiers in chemistry · 2025Article
- Structural Determinants of Redox Conduction Favor Robustness over Tunability in Microbial Cytochrome Nanowires.bioRxiv : the preprint server for biology · 2023Article
- A 300-fold conductivity increase in microbial cytochrome nanowires due to temperature-induced restructuring of hydrogen bonding networks.Science advances · 2022Article
- Contributions to cytochromeChemical science · 2021Article
- Electron-transfer chain in respiratory complex I.Scientific reports · 2017Article
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Authors and funding
3 authors.
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Abstract
Enzymes in biology's energy chains operate with low energy input distributed through multiple electron transfer steps between protein active sites. The general challenge of biological design is how to lower the activation barrier without sacrificing a large negative reaction free energy. We show that this goal is achieved through a large polarizability of the active site. It is polarized by allowing a large number of excited states, which are populated quantum mechanically by electrostatic fluctuations of the protein and hydration water shells. This perspective is achieved by extensive mixed quantum mechanical/molecular dynamics simulations of the half reaction of reduction of cytochrome c. The barrier for electron transfer is consistently lowered by increasing the number of excited states included in the Hamiltonian of the active site diagonalized along the classical trajectory. We suggest that molecular polarizability, in addition to much studied electrostatics of permanent charges, is a key parameter to consider in order to understand how enzymes work.
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