The reactions of heme- and verdoheme-heme oxygenase-1 complexes with FMN-depleted NADPH-cytochrome P450 reductase. Electrons required for verdoheme oxidation can be transferred through a pathway not involving FMN (Q28566694)

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English	The reactions of heme- and verdoheme-heme oxygenase-1 complexes with FMN-depleted NADPH-cytochrome P450 reductase. Electrons required for verdoheme oxidation can be transferred through a pathway not involving FMN	scientific journal article

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scholarly article

1 reference

PubMed publication ID

31 January 2017

The reactions of heme- and verdoheme-heme oxygenase-1 complexes with FMN-depleted NADPH-cytochrome P450 reductase. Electrons required for verdoheme oxidation can be transferred through a pathway not involving FMN (English)

1 reference

PubMed publication ID

31 January 2017

author name string

Yuichiro Higashimoto

1

1 reference

PubMed publication ID

31 January 2017

Hideaki Sato

2

1 reference

PubMed publication ID

31 January 2017

Hiroshi Sakamoto

3

1 reference

PubMed publication ID

31 January 2017

Kenichi Takahashi

4

1 reference

PubMed publication ID

31 January 2017

Graham Palmer

5

1 reference

PubMed publication ID

31 January 2017

Masato Noguchi

6

1 reference

PubMed publication ID

31 January 2017

language of work or name

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publication date

20 October 2006

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PubMed publication ID

31 January 2017

Journal of Biological Chemistry

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PubMed publication ID

31 January 2017

281

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PubMed publication ID

31 January 2017

42

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PubMed publication ID

31 January 2017

31659–31667

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PubMed publication ID

31 January 2017

The mechanism of heme oxygenase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M606163200

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.M606163200

21 January 2018

A kinetic study of the mechanism of conversion of alpha-hydroxyheme to verdoheme while bound to heme oxygenase.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M606163200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M606163200

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.M606163200

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.M606163200

21 January 2018

Electron transfer by diflavin reductases.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M606163200

21 January 2018

Structure and function of NADPH-cytochrome P450 reductase and nitric oxide synthase reductase domain

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M606163200

21 January 2018

Three-dimensional structure of NADPH–cytochrome P450 reductase: Prototype for FMN- and FAD-containing enzymes

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M606163200

21 January 2018

Involvement of NADPH in the interaction between heme oxygenase-1 and cytochrome P450 reductase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M606163200

21 January 2018

Crystal structure of rat apo-heme oxygenase-1 (HO-1): mechanism of heme binding in HO-1 inferred from structural comparison of the apo and heme complex forms

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M606163200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M606163200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M606163200

21 January 2018

Crystal structure of human heme oxygenase-1.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M606163200

21 January 2018

Crystal structure of rat heme oxygenase-1 in complex with biliverdin-iron chelate. Conformational change of the distal helix during the heme cleavage reaction

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M606163200

21 January 2018

Crystal structure of human heme oxygenase-1 in a complex with biliverdin

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M606163200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M606163200

21 January 2018

Regiospecificity determinants of human heme oxygenase: differential NADPH- and ascorbate-dependent heme cleavage by the R183E mutant

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M606163200

21 January 2018

Alteration of the regiospecificity of human heme oxygenase-1 by unseating of the heme but not disruption of the distal hydrogen bonding network

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M606163200

21 January 2018

Purification and characterization of a soluble form of rat liver NADPH-cytochrome P-450 reductase highly expressed in Escherichia coli

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M606163200

21 January 2018

The binding sites on human heme oxygenase-1 for cytochrome p450 reductase and biliverdin reductase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M606163200

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.M606163200

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.M606163200

21 January 2018

The oxidation of hemins by microsomal heme oxygenase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M606163200

21 January 2018

Identifiers

10.1074/JBC.M606163200

1 reference

PubMed publication ID

31 January 2017

PubMed publication ID

1 reference

PubMed publication ID

31 January 2017

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