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The conformation of P450cam in complex with putidaredoxin is dependent on oxidation state.

Abstract:

Double electron-electron resonance (DEER) spectroscopy was used to determine the conformational state in solution for the heme monooxygenase P450cam when bound to its natural redox partner, putidaredoxin (Pdx). When oxidized Pdx was titrated into substrate-bound ferric P450cam, the enzyme shifted from the closed to the open conformation. In sharp contrast, however, the enzyme remained in the closed conformation when ferrous-CO P450cam was titrated with reduced Pdx. This result fully supports ...

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Publication status:
Published

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Publisher copy:
10.1021/ja405751z

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Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Inorganic Chemistry
Goodin, DB More by this author
Journal:
Journal of the American Chemical Society
Volume:
135
Issue:
32
Pages:
11732-11735
Publication date:
2013-08-05
DOI:
EISSN:
1520-5126
ISSN:
0002-7863
URN:
uuid:8adfeffb-a4ba-46ab-9c2e-c0116775a52e
Source identifiers:
428053
Local pid:
pubs:428053

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