Three-dimensional structure of NADPH-cytochrome P450 reductase: Prototype for FMN- and FAD-containing enzymes
Bettie Masters
Proceedings of the National Academy of Sciences, 1997
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A Self-sufficient Cytochrome P450 with a Primary Structural Organization That Includes a Flavin Domain and a [2Fe-2S] Redox Center
Dominic Hunter
Journal of Biological Chemistry, 2003
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Conformational Changes of NADPH-Cytochrome P450 Oxidoreductase Are Essential for Catalysis and Cofactor Binding
Anna Shen
Journal of Biological Chemistry, 2011
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NADPH-Cytochrome P450 Oxidoreductase
Anna Shen
Journal of Biological …, 2001
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The FMN “140s Loop” of Cytochrome P450 Reductase Controls Electron Transfer to Cytochrome P450
Lucy Waskell
International Journal of Molecular Sciences
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Mutants of Cytochrome P450 Reductase Lacking Either Gly-141 or Gly-143 Destabilize Its FMN Semiquinone
Lucy Waskell
The Journal of biological chemistry, 2016
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A second FMN binding site in yeast NADPH-cytochrome P450 reductase suggests a mechanism of electron transfer by diflavin reductases
Valery Yermalitsky
Structure (London, England : 1993), 2006
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Kinetic and Structural Characterization of the Interaction between the FMN Binding Domain of Cytochrome P450 Reductase and Cytochrome c
Lucy Waskell
Journal of Biological Chemistry, 2015
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Inter‐flavin electron transfer in cytochrome P450 reductase – effects of solvent and pH identify hidden complexity in mechanism
Andrew Tyler Munro
The FEBS Journal, 2008
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Cytochrome b5 Inhibits Electron Transfer from NADPH-Cytochrome P450 Reductase to Ferric Cytochrome P450 2B4
Lucy Waskell
Journal of Biological Chemistry, 2008
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Residue 285 in Cytochrome P450 2B4 Lacking the NH2-Terminal Hydrophobic Sequence Has a Role in the Functional Association of NADPH–Cytochrome P450 Reductase
Katharina Tschoep
Biochemical and Biophysical Research Communications, 2000
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Conformational changes of the NADPH-dependent cytochrome P450 reductase in the course of electron transfer to cytochromes P450
Tomas Laursen
Biochimica Et Biophysica Acta-proteins and Proteomics, 2011
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Role of the interface between the FMN and FAD domains in the control of redox potential and electronic transfer of NADPH–cytochrome P450 reductase
Louise Aigrain
Biochemical Journal, 2011
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Probing the Role of the Hinge Segment of Cytochrome P450 Oxidoreductase in the Interaction with Cytochrome P450
Diana Campelo
2018
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The Catalytic Site of Cytochrome P4504A11 (CYP4A11) and Its L131F Mutant
Elizabeth Dierks
Journal of Biological Chemistry, 1998
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The Role of the FMN-Domain of Human Cytochrome P450 Oxidoreductase in Its Promiscuous Interactions With Structurally Diverse Redox Partners
Philippe Urban
Frontiers in Pharmacology
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Determination of the redox potentials and electron transfer properties of the FAD- and FMN-binding domains of the human oxidoreductase NR1
Mark Paine
European Journal of Biochemistry, 2003
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Interaction Modes of Microsomal Cytochrome P450s with Its Reductase and the Role of Substrate Binding
Philippe Urban
International Journal of Molecular Sciences
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Structure of the open conformation of a functional chimeric NADPH cytochrome P450 reductase
Louise Aigrain
EMBO reports, 2009
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Distinct conformational behaviors of four mammalian dual-flavin reductases (cytochrome P450 reductase, methionine synthase reductase, neuronal nitric oxide synthase, endothelial nitric oxide synthase) determine their unique catalytic profiles
Lucy Waskell
FEBS Journal, 2014
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A 31P-nuclear-magnetic-resonance study of NADPH-cytochrome-P-450 reductase and of the Azotobacter flavodoxin/ferredoxin-NADP+ reductase complex
Peter Bonants, Dale Oxidase-edmondson
European Journal of Biochemistry, 1990
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Structure and function of cytochromes P450:a comparative analysis of three crystal structures
Ravi Kurumbail
Structure, 1995
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Electron Transfer Partners of Cytochrome P450
Lucy Waskell
Cytochrome P450
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The three-dimensional structure of NAD(P)H:quinone reductase, a flavoprotein involved in cancer chemoprotection and chemotherapy: mechanism of the two-electron reduction
Rongbao Li
Proceedings of the National Academy of Sciences, 1995
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An overview of the factors playing a role in cytochrome P450 monooxygenase and ferredoxin interactions
Zinhle Chiliza
Biophysical Reviews, 2020
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Electron transfer proteins of cytochrome P450 systems
Israel Hanukoglu
1996
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NADPH P450 oxidoreductase: Structure, function, and pathology of diseases
Amit Pandey
Pharmacology & Therapeutics, 2013
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NADH reduction of nitroaromatics as a probe for residual ferric form high-spin in a cytochrome P450
Maria Pandelia
Biochimica et Biophysica Acta - Proteins and Proteomics, 2018
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Engineering of a functional human NADH-dependent cytochrome P450 system
Mark Paine
Proceedings of the National Academy of Sciences, 2001
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Structural analysis of interactions for complex formation between Ferredoxin-NADP+ reductase and its protein partners
Milagros Medina
Proteins: Structure, Function, and Bioinformatics, 2005
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Thermal inactivation of the reductase domain of cytochrome P450 BM3
Brandon Jeffus, Grover Miller
Archives of Biochemistry and Biophysics, 2005
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One small step for cytochrome P450 in its catalytic cycle, one giant leap for enzymology
Huriye Erdogan
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An Enzymatically Active Chimeric Protein Containing the Hydrophilic Form of NADPH-Cytochrome P450 Reductase Fused to the Membrane-Binding Domain of Cytochrome b5
Sergey Usanov
Biochemical and Biophysical Research Communications, 2001
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