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Open AccessReview

Dynamic Control of Electron Transfers in Diflavin Reductases

Gene Machines Group, Clarendon Laboratory, Department of Physics, University of Oxford, Parks Road, Oxford OX1 3PU, UK
Institut de Chimie des Substances Naturelles, CNRS, UPR 2301, Centre de Recherche de Gif, 1 Av. de la Terrasse, 91198 Gif-sur-Yvette Cedex, France
Université de Toulouse; INSA, UPS, INP; LISBP, 135 Avenue de Rangueil, F-31077 Toulouse, France
Ingénierie des Systèmes Biologiques et des Procédés, F-31400 Toulouse, France
CNRS, UMR5504, F-31400 Toulouse, France
Author to whom correspondence should be addressed.
Int. J. Mol. Sci. 2012, 13(11), 15012-15041;
Received: 8 October 2012 / Revised: 2 November 2012 / Accepted: 13 November 2012 / Published: 15 November 2012
(This article belongs to the Special Issue Flavins)
Diflavin reductases are essential proteins capable of splitting the two-electron flux from reduced pyridine nucleotides to a variety of one electron acceptors. The primary sequence of diflavin reductases shows a conserved domain organization harboring two catalytic domains bound to the FAD and FMN flavins sandwiched by one or several non-catalytic domains. The catalytic domains are analogous to existing globular proteins: the FMN domain is analogous to flavodoxins while the FAD domain resembles ferredoxin reductases. The first structural determination of one member of the diflavin reductases family raised some questions about the architecture of the enzyme during catalysis: both FMN and FAD were in perfect position for interflavin transfers but the steric hindrance of the FAD domain rapidly prompted more complex hypotheses on the possible mechanisms for the electron transfer from FMN to external acceptors. Hypotheses of domain reorganization during catalysis in the context of the different members of this family were given by many groups during the past twenty years. This review will address the recent advances in various structural approaches that have highlighted specific dynamic features of diflavin reductases. View Full-Text
Keywords: diflavin reductases; multidomain proteins; protein dynamics; NOS; CPR; Cytochrome P450 reductase; MSR; NR1; SiR diflavin reductases; multidomain proteins; protein dynamics; NOS; CPR; Cytochrome P450 reductase; MSR; NR1; SiR
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MDPI and ACS Style

Aigrain, L.; Fatemi, F.; Frances, O.; Lescop, E.; Truan, G. Dynamic Control of Electron Transfers in Diflavin Reductases. Int. J. Mol. Sci. 2012, 13, 15012-15041.

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