(Q37964804)

26 August 2017

title

Kinetic and spectroscopic probes of motions and catalysis in the cytochrome P450 reductase family of enzymes (English)

1 reference

26 August 2017

Christopher R Pudney

1

0 references

Sam Hay

object named as

Sam Hay

4

0 references

Derren J Heyes

object named as

Derren J Heyes

2

0 references

Nigel Scrutton

6

object named as

Nigel S Scrutton

1 reference

26 August 2017

Basile Khara

3

1 reference

26 August 2017

Stephen E J Rigby

5

1 reference

26 August 2017

language of work or name

English

0 references

publication date

9 January 2012

1 reference

26 August 2017

1 reference

26 August 2017

volume

279

1 reference

26 August 2017

issue

9

1 reference

26 August 2017

page(s)

1534-1544

1 reference

Enzymatic transition states and dynamic motion in barrier crossing

26 August 2017

cites work

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2011.08442.X

Choreographing an enzyme's dance

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2011.08442.X

The Energy Landscapes and Motions of Proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2011.08442.X

Fluctuating enzymes: lessons from single-molecule studies.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2011.08442.X

A hierarchy of timescales in protein dynamics is linked to enzyme catalysis

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2011.08442.X

Conformational substates modulate hydride transfer in dihydrofolate reductase.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2011.08442.X

Large-scale Domain Dynamics and Adenosylcobalamin Reorientation Orchestrate Radical Catalysis in Ornithine 4,5-Aminomutase

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2011.08442.X

Mutagenesis of morphinone reductase induces multiple reactive configurations and identifies potential ambiguity in kinetic analysis of enzyme tunneling mechanisms

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2011.08442.X

Mechanism of coupled folding and binding of an intrinsically disordered protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2011.08442.X

Intrinsic dynamics of an enzyme underlies catalysis

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2011.08442.X

Hidden alternative structures of proline isomerase essential for catalysis

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2011.08442.X

Extensive conformational sampling in a ternary electron transfer complex

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2011.08442.X

Dynamics driving function: new insights from electron transferring flavoproteins and partner complexes.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2011.08442.X

Structural and mechanistic aspects of flavoproteins: electron transfer through the nitric oxide synthase flavoprotein domain

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2011.08442.X

Conformation-dependent hydride transfer in neuronal nitric oxide synthase reductase domain

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2011.08442.X

Structural basis for isozyme-specific regulation of electron transfer in nitric-oxide synthase.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2011.08442.X

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2011.08442.X

P450 BM3: the very model of a modern flavocytochrome

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2011.08442.X

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2011.08442.X

Inter-flavin electron transfer in cytochrome P450 reductase - effects of solvent and pH identify hidden complexity in mechanism.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2011.08442.X

Electron transfer by diflavin reductases.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2011.08442.X

Stopped-flow kinetic studies of flavin reduction in human cytochrome P450 reductase and its component domains

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2011.08442.X

Structure and Function of an NADPH-Cytochrome P450 Oxidoreductase in an Open Conformation Capable of Reducing Cytochrome P450

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2011.08442.X

Structural basis for human NADPH-cytochrome P450 oxidoreductase deficiency

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2011.08442.X

Role of acidic residues in the interaction of NADPH-cytochrome P450 oxidoreductase with cytochrome P450 and cytochrome c.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2011.08442.X

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2011.08442.X

Conformational Changes of NADPH-Cytochrome P450 Oxidoreductase Are Essential for Catalysis and Cofactor Binding

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2011.08442.X

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2011.08442.X

Laser photoexcitation of NAD(P)H induces reduction of P450 BM3 heme domain on the microsecond time scale

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2011.08442.X

Rapid P450 heme iron reduction by laser photoexcitation of Mycobacterium tuberculosis CYP121 and CYP51B1. Analysis of CO complexation reactions and reversibility of the P450/P420 equilibrium.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2011.08442.X

Demonstration of proton-coupled electron transfer in the copper-containing nitrite reductases

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2011.08442.X

Proton-coupled electron transfer in the catalytic cycle of Alcaligenes xylosoxidans copper-dependent nitrite reductase

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2011.08442.X

Laser flash photolysis studies of the reduction kinetics of NADPH:cytochrome P-450 reductase

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2011.08442.X

Photoinduced intracomplex electron transfer between cytochrome c oxidase and TUPS-modified cytochrome c.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2011.08442.X

Internal electron transfer in multi-site redox enzymes is accessed by laser excitation of thiouredopyrene-3,6,8-trisulfonate (TUPS).

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2011.08442.X

Chapter 28 Use of ruthenium photoreduction techniques to study electron transfer in cytochrome oxidase

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2011.08442.X

Relaxation kinetics of cytochrome P450 reductase: internal electron transfer is limited by conformational change and regulated by coenzyme binding.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2011.08442.X

Electron transfers in chemistry and biology

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2011.08442.X

Protein control of true, gated, and coupled electron transfer reactions.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2011.08442.X

Mechanism of coenzyme binding to human methionine synthase reductase revealed through the crystal structure of the FNR-like module and isothermal titration calorimetry

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2011.08442.X

Parallel pathways and free-energy landscapes for enzymatic hydride transfer probed by hydrostatic pressure

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2011.08442.X

The role of solvent viscosity in the dynamics of protein conformational changes

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2011.08442.X

Kinetic salt effect in pharmaceutical investigations.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2011.08442.X

Coupled motions direct electrons along human microsomal P450 Chains

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2011.08442.X

Impairment of human CYP1A2-mediated xenobiotic metabolism by Antley-Bixler syndrome variants of cytochrome P450 oxidoreductase.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2011.08442.X

Electron transfer by neuronal nitric-oxide synthase is regulated by concerted interaction of calmodulin and two intrinsic regulatory elements

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2011.08442.X

ELDOR Spectroscopy Reveals that Energy Landscapes in Human Methionine Synthase Reductase are Extensively Remodelled Following Ligand and Partner Protein Binding

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2011.08442.X

10.1111/J.1742-4658.2011.08442.X

21 January 2018

Identifiers

DOI

1 reference

26 August 2017

1 reference