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Redox properties of cytochrome p450BM3 measured by direct methods.

Abstract:

Cytochrome p450BM3 is a self-sufficient fatty acid monooxygenase consisting of a diflavin (FAD/FMN) reductase domain and a heme domain fused together in a single polypeptide chain. The multidomain structure makes it an ideal model system for studying the mechanism of electron transfer and for understanding p450 systems in general. Here we report the redox properties of the cytochrome p450BM3 wild-type holoenzyme, and its isolated FAD reductase and p450 heme domains, when immobilized in a dido...

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Publication status:
Published

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Institution:
University of Oxford
Division:
MPLS
Department:
Chemistry
Sub department:
Inorganic Chemistry
Role:
Author
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Journal:
European journal of biochemistry / FEBS
Volume:
270
Issue:
20
Pages:
4082-4088
Publication date:
2003-10-01
DOI:
EISSN:
1432-1033
ISSN:
0014-2956
Source identifiers:
32505
Language:
English
Keywords:
Pubs id:
pubs:32505
UUID:
uuid:078578d9-275c-414e-a8f3-869a89702816
Local pid:
pubs:32505
Deposit date:
2012-12-19

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