Journal article icon

Journal article

Role of the interface between the FMN and FAD domains in the control of redox potential and electronic transfer of NADPH-cytochrome P450 reductase.

Abstract:

CPR (NADPH-cytochrome P450 reductase) is a multidomain protein containing two flavin-containing domains joined by a connecting domain thought to control the necessary movements of the catalytic domains during electronic cycles. We present a detailed biochemical analysis of two chimaeric CPRs composed of the association of human or yeast FMN with the alternative connecting/FAD domains. Despite the assembly of domains having a relatively large evolutionary distance between them, our data suppor...

Expand abstract
Publication status:
Published

Actions


Access Document


Publisher copy:
10.1042/bj20101984

Authors


More by this author
Institution:
University of Oxford
Department:
Oxford, MPLS, Physics
Journal:
The Biochemical journal
Volume:
435
Issue:
1
Pages:
197-206
Publication date:
2011-04-05
DOI:
EISSN:
1470-8728
ISSN:
0264-6021
URN:
uuid:fe759aa6-21a4-4115-b489-a3c1b747b42a
Source identifiers:
155229
Local pid:
pubs:155229

Terms of use


Metrics



If you are the owner of this record, you can report an update to it here: Report update to this record

TO TOP