Journal article
Crystal structure of a ferredoxin reductase for the CYP199A2 system from Rhodopseudomonas palustris.
- Abstract:
-
Cytochrome P450-199A2 from Rhodopseudomonas palustris oxidizes para-substituted benzoic acids and may play a role in lignin and aromatic acid degradation pathways in the bacterium. CYP199A2 has an associated [2Fe-2S] ferredoxin, palustrisredoxin (Pux) but not a ferredoxin reductase. A genome search identified the palustrisredoxin reductase (PuR) gene. PuR was produced in Escherichia coli and shown to be a flavin-dependent protein that supports efficient electron transfer from NADH to Pux, thu...
Expand abstract
- Publication status:
- Published
Actions
Access Document
- Publisher copy:
- 10.1002/prot.22510
Why is the content I wish to access not available via ORA?
Bibliographic data (the information relating to research outputs) and full-text items (e.g. articles, theses, reports, etc.) arrive in ORA from several different sources. Unfortunately we are not able to make available the full-text for every research output.
Please contact the ORA team (
) if you have queries regarding unavailable content OR if you are aware of a full-text copy we can make available.
) if you have queries regarding unavailable content OR if you are aware of a full-text copy we can make available.
Content may be unavailable for the following four reasons
-
Version unsuitable
-
We have not obtained a suitable full-text for a given research output. See this page for more information.
-
Recently completed
-
Sometimes content is held in ORA but is unavailable for a fixed period of time to comply with the policies and wishes of rights holders.
-
Permissions
-
All content made available in ORA should comply with relevant rights, such as copyright. See this page for more information.
-
Clearance
-
Some thesis volumes scanned as part of the digitisation scheme funded by Dr Leonard Polonsky are currently unavailable due to sensitive material or uncleared third-party copyright content. We are attempting to contact authors whose theses are affected.
Alternative access to the full-text
You may be able to access the full-text directly from the publisher's website using the 'Publisher Copy' link in the 'Links & Downloads' box from a research output's ORA record page. This method may require an institutional or individual subscription to the journal/resource.
Authors
Bibliographic Details
- Journal:
- Proteins
- Volume:
- 77
- Issue:
- 4
- Pages:
- 867-880
- Publication date:
- 2009-12-05
- DOI:
- EISSN:
-
1097-0134
- ISSN:
-
0887-3585
- URN:
-
uuid:89948043-64f3-48c4-8c25-b47869de56f2
- Source identifiers:
-
41438
- Local pid:
- pubs:41438
Item Description
- Language:
- English
- Keywords:
Terms of use
- Copyright date:
- 2009
If you are the owner of this record, you can report an update to it here: Report update to this record