Coupling of the distal hydrogen bond network to the exogenous ligand in substrate-bound, resting state human heme oxygenase. - sprookjes - yvandenbroek - TriplyDB

Coupling of the distal hydrogen bond network to the exogenous ligand in substrate-bound, resting state human heme oxygenase.

Coupling of the distal hydrogen bond network to the exogenous ligand in substrate-bound, resting state human heme oxygenase.

http://www.wikidata.org/entity/Q33511502

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Electronic properties of the highly ruffled heme bound to the heme degrading enzyme IsdI.Solution 1H NMR characterization of substrate-free C. diphtheriae heme oxygenase: pertinence for determining magnetic axes in paramagnetic substrate complexes Heme and I.

P2860

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P2860

Coupling of the distal hydrogen bond network to the exogenous ligand in substrate-bound, resting state human heme oxygenase.

http://www.wikidata.org/entity/Q33511502

description

2009 nî lūn-bûn

@nan

2009 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի դեկտեմբերին հրատարակված գիտական հոդված

@hy

2009年の論文

@ja

2009年論文

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2009年論文

@zh-hant

2009年論文

@zh-hk

2009年論文

@zh-mo

2009年論文

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2009年论文

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name

Coupling of the distal hydroge ...... ng state human heme oxygenase.

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Coupling of the distal hydroge ...... ng state human heme oxygenase.

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Coupling of the distal hydroge ...... ng state human heme oxygenase.

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type

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Coupling of the distal hydroge ...... ng state human heme oxygenase.

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Coupling of the distal hydroge ...... ng state human heme oxygenase.

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Coupling of the distal hydroge ...... ng state human heme oxygenase.

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Coupling of the distal hydroge ...... ng state human heme oxygenase.

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Coupling of the distal hydroge ...... ng state human heme oxygenase.

@en

Coupling of the distal hydroge ...... ng state human heme oxygenase.

@nl

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Coupling of the distal hydroge ...... ng state human heme oxygenase.

@en

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Dungeng Peng

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

Gerd N La Mar

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Hiroshi Ogura

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

John P Evans

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Li-Hua Ma

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Paul R Ortiz de Montellano

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

Wenfeng Zhu

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

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Neural roles for heme oxygenase: contrasts to nitric oxide synthase

Comparison of the heme-free and -bound crystal structures of human heme oxygenase-1

Crystal structures of the NO- and CO-bound heme oxygenase from Neisseriae meningitidis. Implications for O2 activation

Crystal structures of the ferric, ferrous, and ferrous-NO forms of the Asp140Ala mutant of human heme oxygenase-1: catalytic implications

Crystal structures of ferrous and CO-, CN(-)-, and NO-bound forms of rat heme oxygenase-1 (HO-1) in complex with heme: structural implications for discrimination between CO and O2 in HO-1

The crystal structures of the ferric and ferrous forms of the heme complex of HmuO, a heme oxygenase of Corynebacterium diphtheriae

Bilirubin is an antioxidant of possible physiological importance

Solution NMR characterization of an unusual distal H-bond network in the active site of the cyanide-inhibited, human heme oxygenase complex of the symmetric substrate, 2,4-dimethyldeuterohemin.

Solution 1H NMR investigation of the active site molecular and electronic structures of substrate-bound, cyanide-inhibited HmuO, a bacterial heme oxygenase from Corynebacterium diphtheriae.

The hydroxide complex of Pseudomonas aeruginosa heme oxygenase as a model of the low-spin iron(III) hydroperoxide intermediate in heme catabolism: 13C NMR spectroscopic studies suggest the active participation of the heme in macrocycle hydroxylation

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11231-11242

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scholarly article

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10.1021/BI901216S

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47

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48

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2009-12-01T00:00:00Z

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38023733

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19842713

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3008551

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