Redox-sensitivity and site-specificity of S- and N- denitrosation in proteins
Redox-sensitivity and site-specificity of S- and N- denitrosation in proteins
We propose that the denitrosation of nitrosated Trp by GSH occurs through homolytic cleavage of nitroso Trp to NO and a Trp aminyl radical, driven by the formation of superoxide derived from the oxidation of GSH to GSSG. Overall, the accessibility of Trp residues to redox-active biomolecules determines the stability of protein-associated nitroso species such that in the case of HSA, N-nitroso-Trp-214 is insensitive to denitrosation by low-molecular-weight antioxidants. Moreover, RNNOs can generate free NO and transfer their NO moiety in an oxygen-dependent fashion, albeit site-specificities appear to differ markedly from that of RSNOs.
e14400-[10pp]
Jourd'heuil, Frances L.
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Lowery, Anthony M.
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Melton, Elaina M.
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Mnaimneh, Sanie
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Bryan, Nathan S.
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Fernandez, Bernadette O.
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Park, Joo-Ho
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Ha, Chung-Eun
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Bhagavan, Nadhipuram V.
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Feelisch, Martin
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Jourd'heuil, David
078be18b-fa42-4a9c-a896-f64c7271bfba
21 December 2010
Jourd'heuil, Frances L.
a5ec8c74-34e7-4bc9-b8ab-055c0623587e
Lowery, Anthony M.
ccecfde9-def9-4996-a33a-121b2ba0d7e6
Melton, Elaina M.
a2565082-19f5-4e7b-848b-0abed686f315
Mnaimneh, Sanie
093bbf8e-515d-48d0-941f-271103d6eff8
Bryan, Nathan S.
709ff51c-c864-4862-9e3f-c5cfd3961025
Fernandez, Bernadette O.
27babc73-7646-4908-86e2-6c29d79fb938
Park, Joo-Ho
61a9c08f-a047-4839-8b41-8e62af6df8be
Ha, Chung-Eun
8cf95acb-5ab5-4e98-8475-f41b833e9ff5
Bhagavan, Nadhipuram V.
7d885d9c-b98c-454d-a6f3-10ed8c65d9a7
Feelisch, Martin
8c1b9965-8614-4e85-b2c6-458a2e17eafd
Jourd'heuil, David
078be18b-fa42-4a9c-a896-f64c7271bfba
Jourd'heuil, Frances L., Lowery, Anthony M., Melton, Elaina M., Mnaimneh, Sanie, Bryan, Nathan S., Fernandez, Bernadette O., Park, Joo-Ho, Ha, Chung-Eun, Bhagavan, Nadhipuram V., Feelisch, Martin and Jourd'heuil, David
(2010)
Redox-sensitivity and site-specificity of S- and N- denitrosation in proteins.
PLoS ONE, 5 (12), .
(doi:10.1371/journal.pone.0014400).
(PMID:21203591)
Abstract
We propose that the denitrosation of nitrosated Trp by GSH occurs through homolytic cleavage of nitroso Trp to NO and a Trp aminyl radical, driven by the formation of superoxide derived from the oxidation of GSH to GSSG. Overall, the accessibility of Trp residues to redox-active biomolecules determines the stability of protein-associated nitroso species such that in the case of HSA, N-nitroso-Trp-214 is insensitive to denitrosation by low-molecular-weight antioxidants. Moreover, RNNOs can generate free NO and transfer their NO moiety in an oxygen-dependent fashion, albeit site-specificities appear to differ markedly from that of RSNOs.
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Published date: 21 December 2010
Organisations:
Clinical & Experimental Sciences
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Local EPrints ID: 337695
URI: http://eprints.soton.ac.uk/id/eprint/337695
ISSN: 1932-6203
PURE UUID: 04ff12e3-71f5-4490-a95e-e728b3541171
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Date deposited: 02 May 2012 12:53
Last modified: 15 Mar 2024 03:41
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Contributors
Author:
Frances L. Jourd'heuil
Author:
Anthony M. Lowery
Author:
Elaina M. Melton
Author:
Sanie Mnaimneh
Author:
Nathan S. Bryan
Author:
Bernadette O. Fernandez
Author:
Joo-Ho Park
Author:
Chung-Eun Ha
Author:
Nadhipuram V. Bhagavan
Author:
David Jourd'heuil
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