Enzymatic and cryoreduction EPR studies of the hydroxylation of methylated N(ω)-hydroxy-L-arginine analogues by nitric oxide synthase from Geobacillus stearothermophilus.

about

Oxygen activation in NO synthases: evidence for a direct role of the substrate Probing the Hydrogen Bonding of the Ferrous-NO Heme Center of nNOS by Pulsed Electron Paramagnetic Resonance.

P2860

Q28833591-80E27F9A-59F3-43A8-8106-31A0CCE5B63B Q42199605-9C722DA0-286D-44CA-8046-3021DE65865F

P2860

Enzymatic and cryoreduction EPR studies of the hydroxylation of methylated N(ω)-hydroxy-L-arginine analogues by nitric oxide synthase from Geobacillus stearothermophilus.

Item

http://www.wikidata.org/entity/Q42953857

description

2014 nî lūn-bûn

@nan

2014年の論文

@ja

2014年論文

@yue

2014年論文

@zh-hant

2014年論文

@zh-hk

2014年論文

@zh-mo

2014年論文

@zh-tw

2014年论文

@wuu

2014年论文

@zh

2014年论文

@zh-cn

name

Enzymatic and cryoreduction EPR studies of the hydroxylation of methylated N

@nl

Enzymatic and cryoreduction EP ...... eobacillus stearothermophilus.

@en

type

Item

label

Enzymatic and cryoreduction EPR studies of the hydroxylation of methylated N

@nl

Enzymatic and cryoreduction EP ...... eobacillus stearothermophilus.

@en

prefLabel

Enzymatic and cryoreduction EPR studies of the hydroxylation of methylated N

@nl

Enzymatic and cryoreduction EP ...... eobacillus stearothermophilus.

@en

P1476

Enzymatic and cryoreduction EP ...... eobacillus stearothermophilus.

@en

P2093

Brian M Hoffman

http://www.w3.org/2001/XMLSchema#string

Brian R Crane

http://www.w3.org/2001/XMLSchema#string

Dmitriy A Lukoyanov

http://www.w3.org/2001/XMLSchema#string

Kristin Jansen Labby

http://www.w3.org/2001/XMLSchema#string

Richard B Silverman

http://www.w3.org/2001/XMLSchema#string

Roman Davydov

http://www.w3.org/2001/XMLSchema#string

Sarah E Chobot

http://www.w3.org/2001/XMLSchema#string

P2860

NO formation by a catalytically self-sufficient bacterial nitric oxide synthase from Sorangium cellulosum

Heme-Coordinating Inhibitors of Neuronal Nitric Oxide Synthase. Iron−Thioether Coordination Is Stabilized by Hydrophobic Contacts without Increased Inhibitor Potency

Methylated N ω -Hydroxy- l -arginine Analogues as Mechanistic Probes for the Second Step of the Nitric Oxide Synthase-Catalyzed Reaction

Nitric oxide synthases: structure, function and inhibition

EPR and ENDOR characterization of the reactive intermediates in the generation of NO by cryoreduced oxy-nitric oxide synthase from Geobacillus stearothermophilus.

Cytochrome P450 compound I: capture, characterization, and C-H bond activation kinetics.

Bacterial flavodoxins support nitric oxide production by Bacillus subtilis nitric-oxide synthase.

Connecting nitrogenase intermediates with the kinetic scheme for N2 reduction by a relaxation protocol and identification of the N2 binding state.

Blocking NO synthesis: how, where and why?

Nitric oxide as a unique signaling molecule in the vascular system: a historical overview.

P304

6511-6519

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1021/BI500485Z

http://www.w3.org/2001/XMLSchema#string

P407

English

P433

http://www.w3.org/2001/XMLSchema#string

P478

http://www.w3.org/2001/XMLSchema#string

P577

2014-10-08T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

266085926

http://www.w3.org/2001/XMLSchema#string

P698

25251261

http://www.w3.org/2001/XMLSchema#string

P932

4204881

http://www.w3.org/2001/XMLSchema#string

Enzymatic and cryoreduction EPR studies of the hydroxylation of methylated N(ω)-hydroxy-L-arginine analogues by nitric oxide synthase from Geobacillus stearothermophilus.

about

P2860

P2860

Enzymatic and cryoreduction EPR studies of the hydroxylation of methylated N(ω)-hydroxy-L-arginine analogues by nitric oxide synthase from Geobacillus stearothermophilus.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P5875

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P5875

P698

P932