Next Article in Journal
Antifungal Activity of (KW)n or (RW)n Peptide against Fusarium solani and Fusarium oxysporum
Next Article in Special Issue
Mutations Associated with Functional Disorder of Xanthine Oxidoreductase and Hereditary Xanthinuria in Humans
Previous Article in Journal
Betulin Complex in γ-Cyclodextrin Derivatives: Properties and Antineoplasic Activities in In Vitro and In Vivo Tumor Models
Previous Article in Special Issue
Role of Key Residues at the Flavin Mononucleotide (FMN):Adenylyltransferase Catalytic Site of the Bifunctional Riboflavin Kinase/Flavin Adenine Dinucleotide (FAD) Synthetase from Corynebacterium ammoniagenes
Int. J. Mol. Sci. 2012, 13(11), 15012-15041; doi:10.3390/ijms131115012
Review

Dynamic Control of Electron Transfers in Diflavin Reductases

1
, 2
, 2
, 2
 and 3,4,5,*
Received: 8 October 2012; in revised form: 2 November 2012 / Accepted: 13 November 2012 / Published: 15 November 2012
(This article belongs to the Special Issue Flavins)
View Full-Text   |   Download PDF [1408 KB, uploaded 19 June 2014]   |   Browse Figures
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.
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
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Export to BibTeX |
EndNote


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.

AMA Style

Aigrain L, Fatemi F, Frances O, Lescop E, Truan G. Dynamic Control of Electron Transfers in Diflavin Reductases. International Journal of Molecular Sciences. 2012; 13(11):15012-15041.

Chicago/Turabian Style

Aigrain, Louise; Fatemi, Fataneh; Frances, Oriane; Lescop, Ewen; Truan, Gilles. 2012. "Dynamic Control of Electron Transfers in Diflavin Reductases." Int. J. Mol. Sci. 13, no. 11: 15012-15041.


Int. J. Mol. Sci. EISSN 1422-0067 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert