title: Dynamic control of electron transfers in diflavin reductases.
abstract: 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.
authors.affiliation: Gene Machines Group, Clarendon Laboratory, Department of Physics, University of Oxford, Parks Road, Oxford OX1 3PU, UK. gilles.truan@insa-toulouse.fr.
authors.forename: Louise
authors.initials: L
authors.lastname: Aigrain
authors.forename: Fataneh
authors.initials: F
authors.lastname: Fatemi
authors.forename: Oriane
authors.initials: O
authors.lastname: Frances
authors.forename: Ewen
authors.initials: E
authors.lastname: Lescop
authors.forename: Gilles
authors.initials: G
authors.lastname: Truan
mesh_terms: D000818:Animals; D004579:Electron Transport / Q000502:physiology*; D038181:FMN Reductase / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D007700:Kinetics; D008958:Models, Molecular; D019001:Nitric Oxide Synthase / Q000378:metabolism; D054730:Protein Interaction Domains and Motifs; D055503:Protein Multimerization
chemical_list: D019001:Nitric Oxide Synthase; D038181:FMN Reductase