Dynamic Control of Electron Transfers in Diflavin Reductases

International Journal of Molecular Sciences

Louise Aigrain¹  Fataneh Fatemi²  Oriane Frances²  Ewen Lescop² 

[1] Gene Machines Group, Clarendon Laboratory, Department of Physics, University of Oxford, Parks Road, Oxford OX1 3PU, UK; E-Mail:;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; E-Mails:

关键词: diflavin reductases;    multidomain proteins;    protein dynamics;    NOS;    CPR;    Cytochrome P450 reductase;    MSR;    NR1;    SiR;   

DOI  :  10.3390/ijms131115012

来源: mdpi

【 摘 要 】

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.

【 授权许可】

CC BY   
© 2012 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland.