Fatty acid metabolism, conformational change, and electron transfer in cytochrome P-450(BM-3). (Q33778025)

29 July 2017

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title

Fatty acid metabolism, conformational change, and electron transfer in cytochrome P-450(BM-3). (English)

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29 July 2017

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H Li

1

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29 July 2017

T L Poulos

series ordinal

2

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29 July 2017

language of work or name

English

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publication date

1 November 1999

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Biochimica et Biophysica Acta

29 July 2017

published in

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29 July 2017

volume

1441

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29 July 2017

issue

2-3

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29 July 2017

page(s)

141-149

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P450 superfamily: update on new sequences, gene mapping, accession numbers and nomenclature.

29 July 2017

cites work

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Hyperpolarizing factors

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A close family resemblance: the importance of structure in understanding cytochromes P450

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Omega-1, Omega-2 and Omega-3 hydroxylation of long-chain fatty acids, amides and alcohols by a soluble enzyme system from Bacillus megaterium

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7 January 2021

The cytochrome P450 4 (CYP4) family

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The highly stereoselective oxidation of polyunsaturated fatty acids by cytochrome P450BM-3

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

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7 January 2021

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

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7 January 2021

An active site substitution, F87V, converts cytochrome P450 BM-3 into a regio- and stereoselective (14S,15R)-arachidonic acid epoxygenase

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7 January 2021

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

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Engineering the substrate specificity of Bacillus megaterium cytochrome P-450 BM3: hydroxylation of alkyl trimethylammonium compounds

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7 January 2021

Dramatic differences in the motions of the mouth of open and closed cytochrome P450BM-3 by molecular dynamics simulations.

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7 January 2021

Redox control of the catalytic cycle of flavocytochrome P-450 BM3.

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7 January 2021

The interaction of cytochrome c and the heme domain of cytochrome P-450BM-3 with the reductase domain of cytochrome P-450BM-3

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7 January 2021

Functional interactions in cytochrome P450BM3. Fatty acid substrate binding alters electron-transfer properties of the flavoprotein domain.

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7 January 2021

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

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7 January 2021

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

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7 January 2021

NMR studies of substrate binding to cytochrome P450 BM3: comparisons to cytochrome P450 cam.

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7 January 2021

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

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7 January 2021

Reconstitution of the fatty acid hydroxylase activity of cytochrome P450BM-3 utilizing its functional domains

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7 January 2021

Equilibrium and transient state spectrophotometric studies of the mechanism of reduction of the flavoprotein domain of P450BM-3.

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7 January 2021

Redox properties of the reduced nicotinamide adenine dinucleotide phosphate-cytochrome P-450 and reduced nicotinamide adenine dinucleotide-cytochrome b5 reductases.

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7 January 2021

Functional Interactions in Cytochrome P450BM3: Flavin Semiquinone Intermediates, Role of NADP(H), and Mechanism of Electron Transfer by the Flavoprotein Domain†

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7 January 2021

Electron transfer between the FMN and heme domains of cytochrome P450BM-3. Effects of substrate and CO.

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7 January 2021

Electrostatic effects of surface acidic amino acid residues on the oxidation-reduction potentials of the flavodoxin from Desulfovibrio vulgaris (Hildenborough).

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7 January 2021

10.1016/S1388-1981(99)00161-4

Identifiers

DOI

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29 July 2017

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