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Biological hydropersulfides and related polysulfides: A new concept and perspective in redox biology

Biological hydropersulfides and related polysulfides: A new concept and perspective in redox biology
Biological hydropersulfides and related polysulfides: A new concept and perspective in redox biology

The chemical biology of thiols (RSH, e.g., cysteine and cysteine containing proteins/peptides) has been a topic of extreme interest for many decades due to their reported roles in protein structure/folding, redox signaling, metal ligation, cellular protection and enzymology. While many of the studies on thiol/sulfur biochemistry have focused on thiols, relatively ignored have been hydropersulfides (RSSH) and higher order polysulfur species (RSSn H, RSSn R, n > 1). Recent and provocative work has alluded to the prevalence and likely physiological importance of RSSH and related RSSn H. RSSH of cysteine (Cys-SSH) has been found to be prevalent in mammalian systems along with Cys-SSH-containing proteins. The RSSH functionality has not been examined to the extent of other biologically relevant sulfur derivatives (e.g., sulfenic acids, disulfides, etc.), whose roles in cell signaling are strongly indicated. The recent finding of Cys-SSH biosynthesis and translational incorporation into proteins is an unequivocal indication of its fundamental importance and necessitates a more profound look into the physiology of RSSH. In this Review, we discuss the currently reported chemical biology of RSSH (and related species) as a prelude to discussing their possible physiological roles. This article is protected by copyright. All rights reserved.

Journal Article, Review
0014-5793
2140-2152
Fukuto, Jon M.
222058bd-beef-4b4e-856c-54b1fc7eb4a9
Ignarro, Louis J.
f25c7aae-94b4-44d9-a726-1483e3d1fd3e
Nagy, Peter
1c1ec453-5922-4e81-ad91-759d512472b7
Wink, David A.
008b5aec-8c2b-4035-8912-fb6fd530413c
Kevil, Christopher G.
1dc237a6-5468-46a9-bb66-c954cb1f005b
Feelisch, Martin
8c1b9965-8614-4e85-b2c6-458a2e17eafd
Cortese-Krott, Miriam Margherita
2d88d4d1-a018-4716-bd54-094b1d016021
Bianco, Christopher L.
cabb8305-5084-4f2e-a877-00ce4314ac07
Kumagai, Yoshito
09eb64f3-169e-4203-bb4f-235e3a44273a
Hobbs, Adrian J.
32179ffa-c3c3-4cf8-96bb-58917dc4c8c0
Lin, Joseph
43812523-2227-4bb2-b963-d4b7ba161a64
Ida, Tomoaki
ebbb63cc-ecd5-4ac7-b3c0-04c6df0963f9
Akaike, Takaaki
3d8928b7-533c-4fd7-b588-dc709f592ba1
Fukuto, Jon M.
222058bd-beef-4b4e-856c-54b1fc7eb4a9
Ignarro, Louis J.
f25c7aae-94b4-44d9-a726-1483e3d1fd3e
Nagy, Peter
1c1ec453-5922-4e81-ad91-759d512472b7
Wink, David A.
008b5aec-8c2b-4035-8912-fb6fd530413c
Kevil, Christopher G.
1dc237a6-5468-46a9-bb66-c954cb1f005b
Feelisch, Martin
8c1b9965-8614-4e85-b2c6-458a2e17eafd
Cortese-Krott, Miriam Margherita
2d88d4d1-a018-4716-bd54-094b1d016021
Bianco, Christopher L.
cabb8305-5084-4f2e-a877-00ce4314ac07
Kumagai, Yoshito
09eb64f3-169e-4203-bb4f-235e3a44273a
Hobbs, Adrian J.
32179ffa-c3c3-4cf8-96bb-58917dc4c8c0
Lin, Joseph
43812523-2227-4bb2-b963-d4b7ba161a64
Ida, Tomoaki
ebbb63cc-ecd5-4ac7-b3c0-04c6df0963f9
Akaike, Takaaki
3d8928b7-533c-4fd7-b588-dc709f592ba1

Fukuto, Jon M., Ignarro, Louis J., Nagy, Peter, Wink, David A., Kevil, Christopher G., Feelisch, Martin, Cortese-Krott, Miriam Margherita, Bianco, Christopher L., Kumagai, Yoshito, Hobbs, Adrian J., Lin, Joseph, Ida, Tomoaki and Akaike, Takaaki (2018) Biological hydropersulfides and related polysulfides: A new concept and perspective in redox biology. FEBS Letters, 592 (12), 2140-2152. (doi:10.1002/1873-3468.13090).

Record type: Review

Abstract

The chemical biology of thiols (RSH, e.g., cysteine and cysteine containing proteins/peptides) has been a topic of extreme interest for many decades due to their reported roles in protein structure/folding, redox signaling, metal ligation, cellular protection and enzymology. While many of the studies on thiol/sulfur biochemistry have focused on thiols, relatively ignored have been hydropersulfides (RSSH) and higher order polysulfur species (RSSn H, RSSn R, n > 1). Recent and provocative work has alluded to the prevalence and likely physiological importance of RSSH and related RSSn H. RSSH of cysteine (Cys-SSH) has been found to be prevalent in mammalian systems along with Cys-SSH-containing proteins. The RSSH functionality has not been examined to the extent of other biologically relevant sulfur derivatives (e.g., sulfenic acids, disulfides, etc.), whose roles in cell signaling are strongly indicated. The recent finding of Cys-SSH biosynthesis and translational incorporation into proteins is an unequivocal indication of its fundamental importance and necessitates a more profound look into the physiology of RSSH. In this Review, we discuss the currently reported chemical biology of RSSH (and related species) as a prelude to discussing their possible physiological roles. This article is protected by copyright. All rights reserved.

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More information

Accepted/In Press date: 30 April 2018
e-pub ahead of print date: 12 May 2018
Published date: June 2018
Keywords: Journal Article, Review

Identifiers

Local EPrints ID: 422099
URI: http://eprints.soton.ac.uk/id/eprint/422099
ISSN: 0014-5793
PURE UUID: 5d4b070e-1e20-4c29-9919-ba1082eeadb1
ORCID for Martin Feelisch: ORCID iD orcid.org/0000-0003-2320-1158

Catalogue record

Date deposited: 16 Jul 2018 16:30
Last modified: 26 Nov 2021 05:10

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Contributors

Author: Jon M. Fukuto
Author: Louis J. Ignarro
Author: Peter Nagy
Author: David A. Wink
Author: Christopher G. Kevil
Author: Martin Feelisch ORCID iD
Author: Miriam Margherita Cortese-Krott
Author: Christopher L. Bianco
Author: Yoshito Kumagai
Author: Adrian J. Hobbs
Author: Joseph Lin
Author: Tomoaki Ida
Author: Takaaki Akaike

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