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Flavin reductase
Biochemical and Biophysical Characterisation of Anopheles Gambiae Nadph-Cytochrome P450 Reductase
Single-Molecule Spectroscopy Reveals How Calmodulin Activates NO Synthase by Controlling Its Conformational Fluctuation Dynamics
View, the Catalytic Center of Bnoss Is Almost Identical to Mnos Except That a Conserved Val Near Heme Iron in Mnos Is Substituted by Iie[25]
Cbic.202000100Taverne
Supplementary Materials
Structural Features That Promote Catalysis in Two-Component Systems Involved in Sulfur Metabolism
On the Natural History of Flavin-Based Electron Bifurcation
Thermostable Flavin Reductase That Couples with Dibenzothiophene Monooxygenase, from Thermophilic Bacillus Sp
A Two-Component Flavin-Dependent Monooxygenase Involved In
Riboflavin: the Health Benefits of a Forgotten Natural Vitamin
82852214.Pdf
Flavins and Flavoproteins 1999
Physical Interaction and Activity Coupling Between Two Enzymes
HANDBOOK of FLAVOPROTEINS Volume 1 Oxidases, Dehydrogenases and Related Systems
Kinetic and Structural Studies on Flavin-Dependent Enzymes Involved in Glycine Betaine Biosynthesis and Propionate 3-Nitronate Detoxification
A Role for Tetrahydrofolates in the Metabolism of Iron-Sulfur Clusters in All Domains of Life
Methylenetetrahydrofolate Reductase: Biochemical Characterization and Medical Significance
AN INTRIGUING FLAVOENZYME INVOLVED in RIBOFLAVIN DEGRADATION a Dissertation by YINDRILA CHAKRABARTY Submitted
Top View
Baeyer-Villiger Monooxygenases Involved in Camphor Degradation
Functional Role for the Conformationally Mobile Phenylalanine 223 in the Reaction of Methylenetetrahydrofolate Reductase from Escherichia Coli†,‡
Eighth Southeast Enzyme Conference
H2 As a Fuel for Flavin- and H2O2-Dependent Biocatalytic Reactions† Cite This: Chem
Molecular Mechanisms of Bacterial Bioluminescence
Seventh Southeast Enzyme Conference
Evolutionary and Molecular Foundations of Multiple
Flavin Oxidoreductase from Escherichia Coli with NADPH
Crystal Structure of Chrr—A Quinone Reductase with the Capacity to Reduce Chromate
Site Directed Mutagenesis of Luxg As a Flavin Reductase from Bioluminescent Bacteria of Photobacterium Leiognathi
Two-Component FAD-Dependent Monooxygenases: Current Knowledge and Biotechnological Opportunities
Structural Basis of Human 5,10-Methylenetetrahydrofolate Reductase (MTHFR) Regulation by Phosphorylation and S-Adenosylmethionine Inhibition
Hexachlorobenzene Monooxygenase Substrate Selectivity and Catalysis
Conformations of Nicotinamide Adenine Dinucleotide (NAD) in Various Environments
The NAD(P)H:Flavin Oxidoreductase from Escherichia
Uva-DARE (Digital Academic Repository)
12 Supplementary Table S1: List of Genes Associated with Detoxification with a Fold Change of 1.5 Or Higher and P-Value Lower Th
The Flavin Reductase Actvb from Streptomyces Coelicolor
On the Diversity of F420-Dependent Oxidoreductases: a Sequence
The Enigmatic Reaction of Flavins with Oxygen Chaiyen, Pimchai; Fraaije, Marco W.; Mattevi, Andrea
Flavin Reductase P: Structure of a Dimeric Enzyme That Reduces Flavin†,‡