Anion-π Interactions in Flavoproteins Involve a Substantial Charge-Transfer Component
| Autor: | Jiří Kozelka, Yevgen P. Yurenko, Radek Marek, Sophia Bazzi |
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| Rok vydání: | 2016 |
| Předmět: |
Anions
Protein Conformation Static Electricity Flavoprotein Flavin group 010402 general chemistry Photochemistry 01 natural sciences Redox Catalysis Cofactor Ion Computational chemistry Flavins Computer Simulation Cysteine Sulfhydryl Compounds Binding Sites biology Flavoproteins 010405 organic chemistry Chemistry Component (thermodynamics) Organic Chemistry Charge (physics) General Chemistry 0104 chemical sciences biology.protein Absorption (chemistry) Oxidation-Reduction Protein Binding |
| Zdroj: | Chemistry (Weinheim an der Bergstrasse, Germany). 23(14) |
| ISSN: | 1521-3765 |
| Popis: | Anion-π interactions have been shown to stabilize flavoproteins and to regulate the redox potential of the flavin cofactor. They are commonly attributed to electrostatic forces. Herein we show that anion-flavin interactions can have a substantial charge-transfer component. Our conclusion emanates from a multi-approach theoretical analysis and is backed by previously reported observations of absorption bands, originating from charge transfer between oxidized flavin and proximate cysteine thiolate groups. This partial covalency of anion-flavin contacts renders classical simulations of flavoproteins questionable. |
| Databáze: | OpenAIRE |
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