Substrate binding favors enhanced NO binding to P450cam.

Substrate binding favors enhanced NO binding to P450cam.

Item
http://www.wikidata.org/entity/Q33200581
Interactions of cytochrome P450s with their ligands.Cytochrome P450–catalyzed L-tryptophan nitration in thaxtomin phytotoxin biosynthesis.Oxidation of methyl and ethyl nitrosamines by cytochrome P450 2E1 and 2B1Thermodynamic characterization of five key kinetic parameters that define neuronal nitric oxide synthase catalysis.Reaction of Mycobacterium tuberculosis cytochrome P450 enzymes with nitric oxide.A "sliding scale rule" for selectivity among NO, CO, and O₂ by heme protein sensors.Spectroscopic and Kinetic Evidence for the Crucial Role of Compound 0 in the P450cam -Catalyzed Hydroxylation of Camphor by Hydrogen Peroxide.Surface plasmon resonance analysis of antifungal azoles binding to CYP3A4 with kinetic resolution of multiple binding orientations.The Ferrous-Dioxygen Intermediate in Human Cytochrome P450 3A4
P2860

Substrate binding favors enhanced NO binding to P450cam.

Item
http://www.wikidata.org/entity/Q33200581
description
2004 nî lūn-bûn
@nan
2004 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
Substrate binding favors enhanced NO binding to P450cam.
@ast
Substrate binding favors enhanced NO binding to P450cam.
@en
type
label
Substrate binding favors enhanced NO binding to P450cam.
@ast
Substrate binding favors enhanced NO binding to P450cam.
@en
prefLabel
Substrate binding favors enhanced NO binding to P450cam.
@ast
Substrate binding favors enhanced NO binding to P450cam.
@en
P1433
P1476
P2093
P304
P31
P356
P407
P433
P478
P577
P698
P356
P1433
P1476
Substrate binding favors enhanced NO binding to P450cam.
@en
P2093
P304
P31
P356
P407
P433
P478
P577
P698