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Infrared spectroscopy provides insight into the role of dioxygen in the nitrosylation pathway of a [2Fe2S] cluster iron-sulfur protein.

Abstract:

We use infrared spectroscopy to demonstrate the critical role that trace O2 plays in determining the products formed when a [2Fe2S] cluster protein reacts with nitric oxide (NO). The observed importance of O2 may have physiological relevance, as many pathogens sense NO using iron-sulfur proteins and will be exposed to NO in an aerobic environment during a mammalian immune response. We show that the [2Fe2S]-containing spinach ferredoxin I undergoes reaction with NO at pH 6.0, with the proporti...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1021/ja505291j

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Institution:
University of Oxford
Division:
MPLS
Department:
Chemistry
Sub department:
Inorganic Chemistry
Role:
Author
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Institution:
University of Oxford
Division:
MPLS
Department:
Chemistry
Sub department:
Inorganic Chemistry
Role:
Author
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Funding agency for:
Ash, P
Grant:
EnergyBioCatalysis-ERC-2010-StG-258600
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Funding agency for:
Vincent, K
Grant:
EP/K031503/1
More from this funder
Funding agency for:
Vincent, K
Grant:
EP/K031503/1
Publisher:
American Chemical Society Publisher's website
Journal:
Journal of the American Chemical Society Journal website
Volume:
136
Issue:
32
Pages:
11236-11239
Publication date:
2014-07-31
DOI:
EISSN:
1520-5126
ISSN:
0002-7863
Source identifiers:
479268
Language:
English
Keywords:
Pubs id:
pubs:479268
UUID:
uuid:4b55f005-b0bd-4ea3-bb5b-bcfa4e2b0bf0
Local pid:
pubs:479268
Deposit date:
2014-08-29

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