ReviewInternational journal of molecular sciences2012
Dynamic control of electron transfers in diflavin reductases.
Review in International journal of molecular sciences, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 26 citations in OpenAlex.
- NADPH-cytochrome P450 reductase mediates P450-dependent metabolic resistance to deltamethrin in Aedes albopictus.Parasites & vectors · 2026Article
- Enzymatic and Biophysical Analysis of two Highly Related Cytochrome P450 Reductases frombioRxiv : the preprint server for biology · 2026Article
- A disease-associated missense mutation in CYP4F3 affects the metabolism of leukotriene B4 via disruption of electron transfer.Journal of cachexia, sarcopenia and muscle · 2022Article
- Ancestral Sequence Reconstruction of a Cytochrome P450 Family Involved in Chemical Defense Reveals the Functional Evolution of a Promiscuous, Xenobiotic-Metabolizing Enzyme in Vertebrates.Molecular biology and evolution · 2022Article
- 19-hydroxy Steroids in the Aromatase Reaction: Review on Expression and Potential Functions.Journal of the Endocrine Society · 2021Review
- A recently evolved diflavin-containing monomeric nitrate reductase is responsible for highly efficient bacterial nitrate assimilation.The Journal of biological chemistry · 2020Article
- Evaluation of Nitrobenzyl Derivatives of Camptothecin as Anti-Cancer Agents and Potential Hypoxia Targeting Prodrugs.Molecules (Basel, Switzerland) · 2018Article
- Direct observation of multiple conformational states in Cytochrome P450 oxidoreductase and their modulation by membrane environment and ionic strength.Scientific reports · 2018Article
- Solution structure of the cytochrome P450 reductase-cytochromeThe Journal of biological chemistry · 2018Article
- Orchestrated Domain Movement in Catalysis by Cytochrome P450 Reductase.Scientific reports · 2017Article
- Article
- Functional characterization of NADPH-cytochrome P450 reductase from Bactrocera dorsalis: Possible involvement in susceptibility to malathion.Scientific reports · 2015Article
- A well-balanced preexisting equilibrium governs electron flux efficiency of a multidomain diflavin reductase.Biophysical journal · 2015Article
- Involvement of Iron-Containing Proteins in Genome Integrity in Arabidopsis Thaliana.Genome integrity · 2015Review
- Article
- Redox-linked domain movements in the catalytic cycle of cytochrome p450 reductase.Structure (London, England : 1993) · 2013Article
Corrections and comments
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Authors and funding
5 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.