(Q46663766)

English

O(2)- and H(2)O(2)-dependent verdoheme degradation by heme oxygenase: reaction mechanisms and potential physiological roles of the dual pathway degradation.

scientific article published on 22 August 2005

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scholarly article

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5 January 2020

O(2)- and H(2)O(2)-dependent verdoheme degradation by heme oxygenase: reaction mechanisms and potential physiological roles of the dual pathway degradation (English)

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:16115896%20AND%20SRC:MED&resulttype=core&format=json

5 January 2020

Toshitaka Matsui

1

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5 January 2020

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Aya Nakajima

2

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5 January 2020

Hiroshi Fujii

3

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5 January 2020

Kathryn Mansfield Matera

4

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5 January 2020

Catharina T Migita

5

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5 January 2020

Tadashi Yoshida

6

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5 January 2020

Masao Ikeda-Saito

7

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publication date

22 August 2005

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5 January 2020

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8

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Journal of Biological Chemistry

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280

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44

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5 January 2020

36833-36840

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5 January 2020

Carbon monoxide: a putative neural messenger

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M503529200

21 January 2018

The heme oxygenase system: a regulator of second messenger gases

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M503529200

21 January 2018

Reduced stress defense in heme oxygenase 1-deficient cells.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M503529200

21 January 2018

The heme oxygenase-carbon monoxide system: a regulator of hepatobiliary function

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M503529200

21 January 2018

Biosynthesis of phycobilins

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M503529200

21 January 2018

The Arabidopsis thaliana HY1 locus, required for phytochrome-chromophore biosynthesis, encodes a protein related to heme oxygenases

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M503529200

21 January 2018

Emerging strategies in microbial haem capture.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M503529200

21 January 2018

Bacterial heme sources: the role of heme, hemoprotein receptors and hemophores

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M503529200

21 January 2018

Reaction intermediates and single turnover rate constants for the oxidation of heme by human heme oxygenase-1.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M503529200

21 January 2018

Verdohemochrome IX alpha: preparation and oxidoreductive cleavage to biliverdin IX alpha

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M503529200

21 January 2018

Formation of a highly oxidized iron biliverdin complex upon treatment of a five-coordinate verdoheme with dioxygen

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M503529200

21 January 2018

Stereoselectivity of each of the three steps of the heme oxygenase reaction: hemin to meso-hydroxyhemin, meso-hydroxyhemin to verdoheme, and verdoheme to biliverdin

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M503529200

21 January 2018

The reactivity of alpha-hydroxyhaem and verdohaem bound to haem oxygenase-1 to dioxygen and sodium dithionite

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M503529200

21 January 2018

Crystal structure of human heme oxygenase-1.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M503529200

21 January 2018

Crystal structure of the dioxygen-bound heme oxygenase from Corynebacterium diphtheriae: implications for heme oxygenase function

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M503529200

21 January 2018

A role for highly conserved carboxylate, aspartate-140, in oxygen activation and heme degradation by heme oxygenase-1.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M503529200

21 January 2018

Catalytic mechanism of heme oxygenase through EPR and ENDOR of cryoreduced oxy-heme oxygenase and its Asp 140 mutants

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M503529200

21 January 2018

Roles of distal Asp in heme oxygenase from Corynebacterium diphtheriae, HmuO: A water-driven oxygen activation mechanism.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M503529200

21 January 2018

Histidine-132 does not stabilize a distal water ligand and is not an important residue for the enzyme activity in heme oxygenase-1.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M503529200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M503529200

21 January 2018

Crystal structure of rat heme oxygenase-1 in complex with heme

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M503529200

21 January 2018

Crystal structures of ferrous and ferrous-NO forms of verdoheme in a complex with human heme oxygenase-1: catalytic implications for heme cleavage

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M503529200

21 January 2018

Proton transfer at helium temperatures during dioxygen activation by heme monooxygenases.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M503529200

21 January 2018

Theory favors a stepwise mechanism of porphyrin degradation by a ferric hydroperoxide model of the active species of heme oxygenase.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M503529200

21 January 2018

Hemoxygenase-2 is an oxygen sensor for a calcium-sensitive potassium channel

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M503529200

21 January 2018

Carbon monoxide neurotransmission activated by CK2 phosphorylation of heme oxygenase-2

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M503529200

21 January 2018

Heme oxygenase-2 is activated by calcium-calmodulin

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M503529200

21 January 2018

Tissue oxygen tension and brain sensitivity to hypoxia

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M503529200

21 January 2018

Heme oxygenase is the major 32-kDa stress protein induced in human skin fibroblasts by UVA radiation, hydrogen peroxide, and sodium arsenite

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M503529200

21 January 2018

Bilirubin, formed by activation of heme oxygenase-2, protects neurons against oxidative stress injury

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M503529200

21 January 2018

Estimation of H2O2 gradients across biomembranes.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M503529200

21 January 2018

Biliverdin reductase: a major physiologic cytoprotectant

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M503529200

21 January 2018

Heme Oxygenase-2

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M503529200

21 January 2018

Identifiers

10.1074/JBC.M503529200

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:16115896%20AND%20SRC:MED&resulttype=core&format=json

5 January 2020

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:16115896%20AND%20SRC:MED&resulttype=core&format=json

5 January 2020

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