Stopped-flow kinetic studies of electron transfer in the reductase domain of neuronal nitric oxide synthase: re-evaluation of the kinetic mechanism reveals new enzyme intermediates and variation with cytochrome P450 reductase.
about
Determination of the redox potentials and electron transfer properties of the FAD- and FMN-binding domains of the human oxidoreductase NR1Kinetic, spectroscopic and thermodynamic characterization of the Mycobacterium tuberculosis adrenodoxin reductase homologue FprACorrelating Calmodulin Landscapes with Chemical Catalysis in Neuronal Nitric Oxide Synthase using Time-Resolved FRET and a 5-Deazaflavin Thermodynamic TrapNADPH-cytochrome P450 oxidoreductase: prototypic member of the diflavin reductase family.Lys842 in neuronal nitric-oxide synthase enables the autoinhibitory insert to antagonize calmodulin binding, increase FMN shielding, and suppress interflavin electron transferStructural and mechanistic aspects of flavoproteins: electron transfer through the nitric oxide synthase flavoprotein domain.Regulation of FMN subdomain interactions and function in neuronal nitric oxide synthaseMechanism of Nitric Oxide Synthase Regulation: Electron Transfer and Interdomain Interactions.A kinetic model linking protein conformational motions, interflavin electron transfer and electron flux through a dual-flavin enzyme-simulating the reductase activity of the endothelial and neuronal nitric oxide synthase flavoprotein domains.Differences in a conformational equilibrium distinguish catalysis by the endothelial and neuronal nitric-oxide synthase flavoproteins.Impeded electron transfer from a pathogenic FMN domain mutant of methionine synthase reductase and its responsiveness to flavin supplementationCharge-pairing interactions control the conformational setpoint and motions of the FMN domain in neuronal nitric oxide synthase.Towards the free energy landscape for catalysis in mammalian nitric oxide synthases.Energy landscapes and catalysis in nitric-oxide synthase.Binding kinetics of calmodulin with target peptides of three nitric oxide synthase isozymes.Magnetic field effects as a result of the radical pair mechanism are unlikely in redox enzymes.A perspective on conformational control of electron transfer in nitric oxide synthases.Conformation-dependent hydride transfer in neuronal nitric oxide synthase reductase domain.Phosphorylation Controls Endothelial Nitric-oxide Synthase by Regulating Its Conformational Dynamics.Dissecting the kinetics of the NADP(+)-FADH2 charge transfer complex and flavin semiquinones in neuronal nitric oxide synthase.Mechanistic studies on the intramolecular one-electron transfer between the two flavins in the human neuronal nitric-oxide synthase and inducible nitric-oxide synthase flavin domains.Interflavin electron transfer in human cytochrome P450 reductase is enhanced by coenzyme binding. Relaxation kinetic studies with coenzyme analogues.The FAD-shielding residue Phe1395 regulates neuronal nitric-oxide synthase catalysis by controlling NADP+ affinity and a conformational equilibrium within the flavoprotein domain.Thermodynamic and kinetic analysis of the isolated FAD domain of rat neuronal nitric oxide synthase altered in the region of the FAD shielding residue Phe1395.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.Cobalamin uptake and reactivation occurs through specific protein interactions in the methionine synthase-methionine synthase reductase complex.The role of a conserved serine residue within hydrogen bonding distance of FAD in redox properties and the modulation of catalysis by Ca2+/calmodulin of constitutive nitric-oxide synthasesElectron transfer by neuronal nitric-oxide synthase is regulated by concerted interaction of calmodulin and two intrinsic regulatory elements
P2860
Q24297622-21C32076-CEA6-4D98-AD5E-5275D288C37FQ28487239-92E2929A-5E48-47AF-B884-62E506B2D768Q28829445-D711E104-A5E9-4A4A-94B4-413694F079B8Q30537968-FCD031BE-4607-4339-A99D-555B3308B4D4Q33661383-87253869-B8A6-44D2-A8AE-6822BDC71331Q33830350-73CBFA68-39CA-41FA-9203-E64B4A2071A8Q33923728-0E2A9E48-B5EC-476C-B62E-6EC4AA6F54C0Q34241528-AE1037E8-4424-4912-A499-8525F745D8BBQ35434947-1AD27235-AF3D-4251-B2C8-AF94D20FFF8CQ36744200-D5A8B153-4F1C-4DAD-BF8F-BAC10224F03AQ37104912-676E12BE-02FA-488D-8605-D2D7F9F61F1BQ37438886-A7D81539-36B3-4534-B299-3FFB01E0CD32Q38285800-90D5C756-F89B-4E76-A6B4-6841326EDCA1Q39006504-90E6E845-E19F-46BE-8FE9-CCFB50D6AFAFQ42026462-15053BD4-8DBC-417D-BC83-6E8B963FD37FQ42126932-6D40DDA8-18E7-4E54-BD6B-D9CAA1594C23Q42323408-EC59B180-AE62-4DF2-A1A1-07CDF08E21A7Q42672439-FB809CDA-435A-424D-83BD-F337296F91F8Q42725750-87DFF774-44C3-4B6A-A2ED-926AAC93255EQ43084509-437F0DF7-C8F2-4D99-B8A8-B633984CB2E0Q44460134-6E6C0C0B-BC63-428A-83AB-618A5502280BQ44465621-02354FD4-92F8-44EE-8BD6-181B48A3F902Q44924216-AC4571C1-DAD5-4913-8499-697C94748308Q44925358-D4885463-B8B5-4CD0-B062-9B05E0458AA3Q46444735-3E106275-D6F9-4D77-853D-1BB6BDBAFD7AQ46693396-5E653731-1477-41E9-9225-D7BED7FD713BQ50335697-75027E60-629B-4EB1-8A94-0FEE9948DCB5Q57217019-789E5F0F-5421-4B4C-9FFD-E039B5873A4DQ57217155-CDD0EB3F-5729-4D0C-968E-BD65223BFFAB
P2860
Stopped-flow kinetic studies of electron transfer in the reductase domain of neuronal nitric oxide synthase: re-evaluation of the kinetic mechanism reveals new enzyme intermediates and variation with cytochrome P450 reductase.
description
2002 nî lūn-bûn
@nan
2002年の論文
@ja
2002年学术文章
@wuu
2002年学术文章
@zh
2002年学术文章
@zh-cn
2002年学术文章
@zh-hans
2002年学术文章
@zh-my
2002年学术文章
@zh-sg
2002年學術文章
@yue
2002年學術文章
@zh-hant
name
Stopped-flow kinetic studies o ...... ith cytochrome P450 reductase.
@en
Stopped-flow kinetic studies o ...... ith cytochrome P450 reductase.
@nl
type
label
Stopped-flow kinetic studies o ...... ith cytochrome P450 reductase.
@en
Stopped-flow kinetic studies o ...... ith cytochrome P450 reductase.
@nl
prefLabel
Stopped-flow kinetic studies o ...... ith cytochrome P450 reductase.
@en
Stopped-flow kinetic studies o ...... ith cytochrome P450 reductase.
@nl
P2860
P356
P1433
P1476
Stopped-flow kinetic studies o ...... ith cytochrome P450 reductase.
@en
P2093
Kirsty Knight
Nigel S Scrutton
P2860
P356
10.1042/BJ20020667
P407
P577
2002-10-01T00:00:00Z