An unusual yet strongly conserved flavoprotein reductase in bacteria and mammals.
about
Crystal structure of the FMN-binding domain of human cytochrome P450 reductase at 1.93 A resolutionDetermination of the redox potentials and electron transfer properties of the FAD- and FMN-binding domains of the human oxidoreductase NR1Structure of a cytochrome P450-redox partner electron-transfer complexThe crystal structure of the FAD/NADPH-binding domain of flavocytochrome P450 BM3Structure and Biochemical Properties of the Alkene Producing Cytochrome P450 OleTJE(CYP152L1) from theJeotgalicoccussp. 8456 BacteriumNeuronal calcium sensor protein visinin-like protein-3 interacts with microsomal cytochrome b5 in a Ca2+-dependent mannerA conserved aspartate (Asp-1393) regulates NADPH reduction of neuronal nitric-oxide synthase: implications for catalysisThe flavin reductase activity of the flavoprotein component of sulfite reductase from Escherichia coli. A new model for the protein structure.Structurally and functionally conserved regions of cytochrome P-450 reductase as targets for DNA amplification by the polymerase chain reaction. Cloning and nucleotide sequence of the Schizosaccharomyces pombe cDNAThe P450 oxidoreductase, RedA, controls development beyond the mound stage in Dictyostelium discoideum.Cytochrome P450-based cancer gene therapy: recent advances and future prospects.Structural and mechanistic aspects of flavoproteins: electron transfer through the nitric oxide synthase flavoprotein domain.The autoinhibitory control element and calmodulin conspire to provide physiological modulation of endothelial and neuronal nitric oxide synthase activity.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.Bacterial flavodoxins support nitric oxide production by Bacillus subtilis nitric-oxide synthase.Studies on the redox centers of the terminal oxidase from Desulfovibrio gigas and evidence for its interaction with rubredoxin.Cloning, characterization and import studies on protochlorophyllide reductase from wheat (Triticum aestivum).Cytochrome P450/redox partner fusion enzymes: biotechnological and toxicological prospects.Crystallization and preliminary x-ray diffraction analysis of P450terp and the hemoprotein domain of P450BM-3, enzymes belonging to two distinct classes of the cytochrome P450 superfamilyCloned, expressed rat cerebellar nitric oxide synthase contains stoichiometric amounts of heme, which binds carbon monoxide.P450(BM3) (CYP102A1): connecting the dots.Role of acidic residues in the interaction of NADPH-cytochrome P450 oxidoreductase with cytochrome P450 and cytochrome c.Probing the NADPH-binding site of Escherichia coli flavodoxin oxidoreductase.Photosynthetic fuel for heterologous enzymes: the role of electron carrier proteins.Cytochrome b-245 is a flavocytochrome containing FAD and the NADPH-binding site of the microbicidal oxidase of phagocytes.The FMN to heme electron transfer in cytochrome P450BM-3. Effect of chemical modification of cysteines engineered at the FMN-heme domain interaction site.Induction of cytochrome P-450 BM-3 (CYP 102) by non-steroidal anti-inflammatory drugs in Bacillus megaterium.Identification of the domains of neuronal nitric oxide synthase by limited proteolysis.An autoinhibitory control element defines calcium-regulated isoforms of nitric oxide synthase.Modification of the nucleotide cofactor-binding site of cytochrome P-450 reductase to enhance turnover with NADH in Vivo.Interflavin electron transfer in human cytochrome P450 reductase is enhanced by coenzyme binding. Relaxation kinetic studies with coenzyme analogues.Distinguishing two groups of flavin reductases by analyzing the protonation state of an active site carboxylic acid.The domain architecture of cytochrome P450BM-3.Inter-flavin electron transfer in cytochrome P450 reductase - effects of solvent and pH identify hidden complexity in mechanism.C-terminal tail residue Arg1400 enables NADPH to regulate electron transfer in neuronal nitric-oxide synthase.Interaction between the reductase Tah18 and highly conserved Fe-S containing Dre2 C-terminus is essential for yeast viabilityMechanism of cytochrome P450 reductase from the house fly: evidence for an FMN semiquinone as electron donor.Structural and enzymological analysis of the interaction of isolated domains of cytochrome P-450 BM3.
P2860
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P2860
An unusual yet strongly conserved flavoprotein reductase in bacteria and mammals.
description
1991 nî lūn-bûn
@nan
1991 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1991 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1991年の論文
@ja
1991年論文
@yue
1991年論文
@zh-hant
1991年論文
@zh-hk
1991年論文
@zh-mo
1991年論文
@zh-tw
1991年论文
@wuu
name
An unusual yet strongly conserved flavoprotein reductase in bacteria and mammals.
@ast
An unusual yet strongly conserved flavoprotein reductase in bacteria and mammals.
@en
An unusual yet strongly conserved flavoprotein reductase in bacteria and mammals.
@nl
type
label
An unusual yet strongly conserved flavoprotein reductase in bacteria and mammals.
@ast
An unusual yet strongly conserved flavoprotein reductase in bacteria and mammals.
@en
An unusual yet strongly conserved flavoprotein reductase in bacteria and mammals.
@nl
prefLabel
An unusual yet strongly conserved flavoprotein reductase in bacteria and mammals.
@ast
An unusual yet strongly conserved flavoprotein reductase in bacteria and mammals.
@en
An unusual yet strongly conserved flavoprotein reductase in bacteria and mammals.
@nl
P1476
An unusual yet strongly conserved flavoprotein reductase in bacteria and mammals.
@en
P2093
P304
P356
10.1016/0968-0004(91)90059-5
P577
1991-04-01T00:00:00Z