Trisulfides in Proteins

Rasmus W. Nielsen; Christine Tachibana; Niels Erik Hansen; Jakob R Winther

doi:10.1089/ars.2010.3677

Trisulfides in Proteins

Rasmus W. Nielsen, Christine Tachibana, Niels Erik Hansen, Jakob R Winther

Biomolecular Sciences

39 Citationer (Scopus)

Abstract

Trisulfides and other oligosulfides are widely distributed in the biological world. In plants, for example, garlic, trisulfides are associated with potentially beneficial properties. However, an extra neutral sulfur atom covalently bound between the two sulfur atoms of a pair of cysteines is not a common post-translational modification, and the number of proteins in which a trisulfide has been unambiguously identified is small. Nevertheless, we believe that its prevalence may be underestimated, particularly with the increasing evidence for significant pools of sulfides in living tissues and their possible roles in cellular metabolism. This review focuses on examples of proteins that are known to contain a trisulfide bridge, and gives an overview of the chemistry of trisulfide formation, and the methods by which it is detected in proteins.

Originalsprog	Engelsk
Tidsskrift	Antioxidants & Redox Signaling
Vol/bind	15
Udgave nummer	1
Sider (fra-til)	67-75
Antal sider	9
ISSN	1523-0864
DOI	https://doi.org/10.1089/ars.2010.3677
Status	Udgivet - 1 jul. 2011

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10.1089/ars.2010.3677

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abstract = "Trisulfides and other oligosulfides are widely distributed in the biological world. In plants, for example, garlic, trisulfides are associated with potentially beneficial properties. However, an extra neutral sulfur atom covalently bound between the two sulfur atoms of a pair of cysteines is not a common post-translational modification, and the number of proteins in which a trisulfide has been unambiguously identified is small. Nevertheless, we believe that its prevalence may be underestimated, particularly with the increasing evidence for significant pools of sulfides in living tissues and their possible roles in cellular metabolism. This review focuses on examples of proteins that are known to contain a trisulfide bridge, and gives an overview of the chemistry of trisulfide formation, and the methods by which it is detected in proteins.",

author = "Nielsen, {Rasmus W.} and Christine Tachibana and Hansen, {Niels Erik} and Winther, {Jakob R}",

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TY - JOUR

T1 - Trisulfides in Proteins

AU - Nielsen, Rasmus W.

AU - Tachibana, Christine

AU - Hansen, Niels Erik

AU - Winther, Jakob R

PY - 2011/7/1

Y1 - 2011/7/1

N2 - Trisulfides and other oligosulfides are widely distributed in the biological world. In plants, for example, garlic, trisulfides are associated with potentially beneficial properties. However, an extra neutral sulfur atom covalently bound between the two sulfur atoms of a pair of cysteines is not a common post-translational modification, and the number of proteins in which a trisulfide has been unambiguously identified is small. Nevertheless, we believe that its prevalence may be underestimated, particularly with the increasing evidence for significant pools of sulfides in living tissues and their possible roles in cellular metabolism. This review focuses on examples of proteins that are known to contain a trisulfide bridge, and gives an overview of the chemistry of trisulfide formation, and the methods by which it is detected in proteins.

AB - Trisulfides and other oligosulfides are widely distributed in the biological world. In plants, for example, garlic, trisulfides are associated with potentially beneficial properties. However, an extra neutral sulfur atom covalently bound between the two sulfur atoms of a pair of cysteines is not a common post-translational modification, and the number of proteins in which a trisulfide has been unambiguously identified is small. Nevertheless, we believe that its prevalence may be underestimated, particularly with the increasing evidence for significant pools of sulfides in living tissues and their possible roles in cellular metabolism. This review focuses on examples of proteins that are known to contain a trisulfide bridge, and gives an overview of the chemistry of trisulfide formation, and the methods by which it is detected in proteins.

U2 - 10.1089/ars.2010.3677

DO - 10.1089/ars.2010.3677

M3 - Journal article

C2 - 20977350

SN - 1523-0864

VL - 15

SP - 67

EP - 75

JO - Antioxidants & Redox Signaling

JF - Antioxidants & Redox Signaling

IS - 1

ER -

Trisulfides in Proteins

Abstract

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