A single mutation in cytochrome P450 BM3 induces the conformational rearrangement seen upon substrate binding in the wild-type enzyme. (Q44799693)

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25 December 2019

title

A single mutation in cytochrome P450 BM3 induces the conformational rearrangement seen upon substrate binding in the wild-type enzyme (English)

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25 December 2019

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25 December 2019

M Gordon Joyce

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25 December 2019

Hazel M Girvan

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25 December 2019

David Leys

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25 December 2019

language of work or name

English

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publication date

12 March 2004

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Journal of Biological Chemistry

25 December 2019

published in

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volume

279

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issue

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25 December 2019

page(s)

23287-23293

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Update information on human P450s

25 December 2019

cites work

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21 January 2018

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P450BM-3 and other inducible bacterial P450 cytochromes: biochemistry and regulation

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Redox Control of the Catalytic Cycle of Flavocytochrome P-450 BM3

21 January 2018

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Coupling of spin, substrate, and redox equilibriums in cytochrome P450

21 January 2018

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The structure of the cytochrome p450BM-3 haem domain complexed with the fatty acid substrate, palmitoleic acid

21 January 2018

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Crystal structures of ligand complexes of P450eryF exhibiting homotropic cooperativity

21 January 2018

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High-resolution crystal structure of cytochrome P450cam

21 January 2018

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Pivotal role of water in the mechanism of P450BM-3

21 January 2018

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Crystal structure of cytochrome P450 14 -sterol demethylase (CYP51) from Mycobacterium tuberculosis in complex with azole inhibitors

21 January 2018

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Atomic structure of Mycobacterium tuberculosis CYP121 to 1.06 A reveals novel features of cytochrome P450

21 January 2018

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Crystal structures of cytochrome P-450CAM complexed with camphane, thiocamphor, and adamantane: factors controlling P-450 substrate hydroxylation

21 January 2018

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Crystal structure of hemoprotein domain of P450BM-3, a prototype for microsomal P450's

21 January 2018

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Autocatalytic radical reactions in physiological prosthetic heme modification

21 January 2018

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Flavocytochrome P450 BM3 mutant A264E undergoes substrate-dependent formation of a novel heme iron ligand set.

21 January 2018

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Processing of X-ray diffraction data collected in oscillation mode

21 January 2018

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Refinement of macromolecular structures by the maximum-likelihood method

21 January 2018

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Flavocytochrome P-450 BM3: a paradigm for the analysis of electron transfer and its control in the P-450s

21 January 2018

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Cytochrome P450 4A fatty acid omega hydroxylases

21 January 2018

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Substrate recognition and molecular mechanism of fatty acid hydroxylation by cytochrome P450 from Bacillus subtilis. Crystallographic, spectroscopic, and mutational studies

21 January 2018

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Domains of the catalytically self-sufficient cytochrome P-450 BM-3. Genetic construction, overexpression, purification and spectroscopic characterization

21 January 2018

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Antifungals: mechanism of action and resistance, established and novel drugs

21 January 2018

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Phenylalanine 393 exerts thermodynamic control over the heme of flavocytochrome P450 BM3.

21 January 2018

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A Single Mutation in Cytochrome P450 BM3 Changes Substrate Orientation in a Catalytic Intermediate and the Regiospecificity of Hydroxylation†

21 January 2018

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1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine as a Substrate of Cytochrome P450 2D6: Allosteric Effects of NADPH−Cytochrome P450 Reductase†

21 January 2018

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The catalytic mechanism of cytochrome P450 BM3 involves a 6 Å movement of the bound substrate on reduction

21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.M401717200

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15020590%20AND%20SRC:MED&resulttype=core&format=json

25 December 2019

1 reference

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