Neutralizing a surface charge on the FMN subdomain increases the activity of neuronal nitric-oxide synthase by enhancing the oxygen reactivity of the enzyme heme-nitric oxide complex

Neutralizing a surface charge on the FMN subdomain increases the activity of neuronal nitric-oxide synthase by enhancing the oxygen reactivity of the enzyme heme-nitric oxide complex

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http://www.wikidata.org/entity/Q37339263
A bridging interaction allows calmodulin to activate NO synthase through a bi-modal mechanismRegulation of interdomain electron transfer in the NOS output state for NO productionPulsed EPR determination of the distance between heme iron and FMN centers in a human inducible nitric oxide synthase.Lys842 in neuronal nitric-oxide synthase enables the autoinhibitory insert to antagonize calmodulin binding, increase FMN shielding, and suppress interflavin electron transferSurface charges and regulation of FMN to heme electron transfer in nitric-oxide synthase.Molecular architecture of mammalian nitric oxide synthases.Mechanism of Nitric Oxide Synthase Regulation: Electron Transfer and Interdomain Interactions.Regulatory role of Glu546 in flavin mononucleotide-heme electron transfer in human inducible nitric oxide synthase.Mutation in the flavin mononucleotide domain modulates magnetic circular dichroism spectra of the iNOS ferric cyano complex in a substrate-specific manner.Control of electron transfer and catalysis in neuronal nitric-oxide synthase (nNOS) by a hinge connecting its FMN and FAD-NADPH domains.Insight into structural rearrangements and interdomain interactions related to electron transfer between flavin mononucleotide and heme in nitric oxide synthase: A molecular dynamics studyThermodynamic characterization of five key kinetic parameters that define neuronal nitric oxide synthase catalysis.Nitric oxide synthase domain interfaces regulate electron transfer and calmodulin activation.Dissecting regulation mechanism of the FMN to heme interdomain electron transfer in nitric oxide synthases.Charge-pairing interactions control the conformational setpoint and motions of the FMN domain in neuronal nitric oxide synthase.Tetrahydrobiopterin redox cycling in nitric oxide synthase: evidence supports a through-heme electron delivery.A Cross-Domain Charge Interaction Governs the Activity of NO Synthase.
P2860

Neutralizing a surface charge on the FMN subdomain increases the activity of neuronal nitric-oxide synthase by enhancing the oxygen reactivity of the enzyme heme-nitric oxide complex

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http://www.wikidata.org/entity/Q37339263
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 27 May 2009
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Neutralizing a surface charge ...... zyme heme-nitric oxide complex
@en
Neutralizing a surface charge ...... yme heme-nitric oxide complex.
@nl
type
label
Neutralizing a surface charge ...... zyme heme-nitric oxide complex
@en
Neutralizing a surface charge ...... yme heme-nitric oxide complex.
@nl
prefLabel
Neutralizing a surface charge ...... zyme heme-nitric oxide complex
@en
Neutralizing a surface charge ...... yme heme-nitric oxide complex.
@nl
P1433
P1476
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P698
P932
P356
P1433
P1476
Neutralizing a surface charge ...... zyme heme-nitric oxide complex
@en
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P698
P932