The crystal structure of the FAD/NADPH-binding domain of flavocytochrome P450 BM3 (Q27677419)

6

object named as

Hazel M Girvan

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author name string

Michael G Joyce

1

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Idorenyin S Ekanem

2

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Olivier Roitel

3

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Adrian J Dunford

4

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Rajasekhar Neeli

5

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George J Baker

7

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Robin A Curtis

8

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Andrew W Munro

P450 BM3: the very model of a modern flavocytochrome

9

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language of work or name

English

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publication date

May 2012

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published in

FEBS Journal

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volume

279

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issue

9

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page(s)

1694-706

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cites work

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Roles of key active-site residues in flavocytochrome P450 BM3

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The dimeric form of flavocytochrome P450 BM3 is catalytically functional as a fatty acid hydroxylase.

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

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

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Structural and spectroscopic characterization of P450 BM3 mutants with unprecedented P450 heme iron ligand sets. New heme ligation states influence conformational equilibria in P450 BM3.

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Identifiers

DOI

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Fatcat ID

release_4khx4za27fgpnigaggis77gmqu

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Fatcat

https://api.fatcat.wiki/v0/release/4khx4za27fgpnigaggis77gmqu