Domain motion in cytochrome P450 reductase: conformational equilibria revealed by NMR and small-angle x-ray scattering. (Q41897409)

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11 February 2020

title

Domain motion in cytochrome P450 reductase: conformational equilibria revealed by NMR and small-angle x-ray scattering (English)

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X-ray scattering techniques

11 February 2020

main subject

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4

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11 February 2020

Gordon Roberts

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11 February 2020

3

Igor L Barsukov

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11 February 2020

author name string

Jacqueline Ellis

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11 February 2020

Aldo Gutierrez

2

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11 February 2020

J Günter Grossmann

5

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11 February 2020

language of work or name

English

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publication date

26 October 2009

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Journal of Biological Chemistry

11 February 2020

published in

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11 February 2020

volume

284

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issue

52

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11 February 2020

page(s)

36628-36637

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Structure of the open conformation of a functional chimeric NADPH cytochrome P450 reductase

11 February 2020

cites work

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Differences in a conformational equilibrium distinguish catalysis by the endothelial and neuronal nitric-oxide synthase flavoproteins.

5 June 2018

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Structural characterization of flexible proteins using small-angle X-ray scattering

5 June 2018

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

5 June 2018

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Single-molecule height measurements on microsomal cytochrome P450 in nanometer-scale phospholipid bilayer disks

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Mapping the interactions between flavodoxin and its physiological partners flavodoxin reductase and cobalamin-dependent methionine synthase

5 June 2018

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Involvement of NADPH: cytochrome P450 reductase in the activation of indoloquinone EO9 to free radical and DNA damaging species

5 June 2018

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NADPH-cytochrome P450 oxidoreductase. Structural basis for hydride and electron transfer

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Four crystal structures of the 60 kDa flavoprotein monomer of the sulfite reductase indicate a disordered flavodoxin-like module

5 June 2018

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Cloning and characterization of a novel human dual flavin reductase

5 June 2018

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Structure of a cytochrome P450-redox partner electron-transfer complex

5 June 2018

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Crystal structure of the FMN-binding domain of human cytochrome P450 reductase at 1.93 A resolution

5 June 2018

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Cloning and mapping of a cDNA for methionine synthase reductase, a flavoprotein defective in patients with homocystinuria

5 June 2018

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

5 June 2018

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5 June 2018

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Dissection of NADPH-cytochrome P450 oxidoreductase into distinct functional domains

5 June 2018

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5 June 2018

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Immunochemical evidence for an association of heme oxygenase with the microsomal electron transport system.

5 June 2018

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5 June 2018

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Cytochrome b5 reduction by NADPH-cytochrome P-450 reductase

5 June 2018

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5 June 2018

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Global effects of the energetics of coenzyme binding: NADPH controls the protein interaction properties of human cytochrome P450 reductase.

18 August 2018

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18 August 2018

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18 August 2018

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18 August 2018

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18 August 2018

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18 August 2018

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18 August 2018

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21 January 2018

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21 January 2018

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The relative importance of NADPH: cytochrome c (P450) reductase for determining the sensitivity of human tumour cells to the indolequinone EO9 and related analogues lacking functionality at the C-2 and C-3 positions

21 January 2018

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1H, 15N and 13C NMR resonance assignment, secondary structure and global fold of the FMN-binding domain of human cytochrome P450 reductase

21 January 2018

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Conformational dynamics and the energetics of protein--ligand interactions: role of interdomain loop in human cytochrome P450 reductase

21 January 2018

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12 December 2020

Evidence for a new physiological role of hepatic NADPH:ferricytochrome (P-450) oxidoreductase. Direct electron input to the microsomal fatty acid chain elongation system

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12 December 2020

NADPH-cytochrome P-450 oxidoreductase: flavin mononucleotide and flavin adenine dinucleotide domains evolved from different flavoproteins

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12 December 2020

Interaction with arginine 597 of NADPH-cytochrome P-450 oxidoreductase is a primary source of the uniform binding energy used to discriminate between NADPH and NADH

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Cold-inducible cloning vectors for low-temperature protein expression in Escherichia coli: application to the production of a toxic and proteolytically sensitive fusion protein

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Identifiers

DOI

10.1074/JBC.M109.054304

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:19858215%20AND%20SRC:MED&resulttype=core&format=json

11 February 2020

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11 February 2020

PubMed publication ID

19858215

1 reference