Anion-pi interactions in flavoproteins involve a substantial charge-transfer component

YURENKO, Yevgen, Sophia BAZZI, Radek MAREK and Jiří KOZELKA. Anion-pi interactions in flavoproteins involve a substantial charge-transfer component. Chemistry - A European Journal. Weinheim, Germany: Wiley-VCH, 2017, vol. 23, No 14, p. 3246-3250, 6 pp. ISSN 0947-6539. doi:10.1002/chem.201605307.

Basic information

• Original name: Anion-pi interactions in flavoproteins involve a substantial charge-transfer component
• Authors: YURENKO, Yevgen (804 Ukraine, belonging to the institution), Sophia BAZZI (364 Islamic Republic of Iran), Radek MAREK (203 Czech Republic, belonging to the institution) and Jiří KOZELKA (250 France, belonging to the institution).
• Edition: Chemistry - A European Journal, Weinheim, Germany, Wiley-VCH, 2017, 0947-6539.

Other information

• Original language: English
• Type of outcome: Article in a journal
• Field of Study: 10403 Physical chemistry
• Country of publisher: Germany
• Confidentiality degree: is not subject to a state or trade secret
• WWW: DOI: 10.1002/chem.201605307
• Impact factor: Impact factor: 5.160
• RIV identification code: RIV/00216224:14310/17:00094613
• Organization unit: Faculty of Science
• Doi: http://dx.doi.org/10.1002/chem.201605307
• UT WoS: 000395775700002
• Keywords in English: covalence; charge-transfer component; energy decomposition
• Tags: NZ, rivok
• Tags: International impact, Reviewed

Abstract

Anion-pi interactions have been shown to stabilize flavoproteins and to regulate the redox potential of the flavin cofactor. They are commonly attributed to electrostatic forces. Here we show that anion-flavin interactions have a substantial charge-transfer component. Our conclusion emanates from a multiapproach theoretical analysis and is backed by previously reported observations of absorption bands, originating from charge transfer between oxidized flavin and proximate cystein thiolate groups. This partial covalency of anion-flavin contacts renders classical simulations of flavoproteins questionable.

Links

• GA14-14654S, research and development project: Name: Studium fyzikální podstaty interakcí lone-pair-pi v biomolekulárních systémech. Role interakcí lone-pair-pi při stabilizaci proteinu Engrailed (Acronym: Lone-pair-pi interactions)

Investor: Czech Science Foundation

• LQ1601, research and development project: Name: CEITEC 2020 (Acronym: CEITEC2020)

Investor: Ministry of Education, Youth and Sports of the CR