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Journal article

Dioxygen controls the nitrosylation reactions of a protein-bound [4Fe4S] cluster

Abstract:

Iron–sulfur clusters are exceptionally tuneable protein cofactors, and as one of their many roles they are involved in biological responses to nitrosative stress. Both iron–sulfur proteins and synthetic model clusters are extremely sensitive to nitrosylation, tending towards rapid multi-step reaction and cluster degradation. Reaction of protein-bound iron–sulfur clusters with nitric oxide can be stopped at partial nitrosylation in vivo, and repair of protein-bound nitrosylated clusters is pos...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1039/C9DT00924H

Authors


More by this author
Institution:
University of Oxford
Division:
MPLS Division
Department:
Chemistry
Sub department:
Inorganic Chemistry
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MPLS Division
Department:
Chemistry
Sub department:
Inorganic Chemistry
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MPLS
Department:
Chemistry
Sub department:
Inorganic Chemistry
Oxford college:
Jesus College
Role:
Author
Publisher:
Royal Society of Chemistry Publisher's website
Journal:
Dalton Transactions Journal website
Volume:
48
Issue:
37
Pages:
13960-13970
Publication date:
2019-09-09
Acceptance date:
2019-08-14
DOI:
EISSN:
1477-9234
ISSN:
1477-9226
Source identifiers:
1045658
Keywords:
Pubs id:
pubs:1045658
UUID:
uuid:2b2bd264-2264-4bd8-a535-fec60803ccf0
Local pid:
pubs:1045658
Deposit date:
2019-08-15

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