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Protein recognition in ferredoxin-P450 electron transfer in the class I CYP199A2 system from Rhodopseudomonas palustris.

Abstract:

CYP199A2 from Rhodopseudomonas palustris CGA009 is a heme monooxygenase that catalyzes the oxidation of para-substituted benzoic acids. CYP199A2 activity is reconstituted by a class I electron transfer chain consisting of the associated [2Fe-2S] ferredoxin palustrisredoxin (Pux) and a flavoprotein palustrisredoxin reductase (PuR). Another [2Fe-2S] ferredoxin, palustrisredoxin B (PuxB; RPA3956) has been identified in the genome. PuxB shares sequence identity and motifs with vertebrate-type fer...

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Publication status:
Published

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Publisher copy:
10.1007/s00775-009-0604-7

Authors


Johnson, EO More by this author
Forward, IM More by this author
Bartlam, M More by this author
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Journal:
Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry
Volume:
15
Issue:
3
Pages:
315-328
Publication date:
2010-03-05
DOI:
EISSN:
1432-1327
ISSN:
0949-8257
URN:
uuid:01e20eb4-8fab-458d-bb00-b3b34aa23811
Source identifiers:
34969
Local pid:
pubs:34969

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