Abstract
| Originalsprog | Engelsk |
|---|---|
| Tidsskrift | Antioxidants & Redox Signaling |
| Vol/bind | 11 |
| Udgave nummer | 5 |
| Sider (fra-til) | 1047-1058 |
| ISSN | 1523-0864 |
| DOI | |
| Status | Udgivet - 2009 |
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Kinetic and Thermodynamic Aspects of Cellular Thiol-Disulfide Redox Regulation. / Jensen, Kristine Steen; Hansen, Rosa Erritzøe; Winther, Jakob R.
I: Antioxidants & Redox Signaling, Bind 11, Nr. 5, 2009, s. 1047-1058.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › peer review
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TY - JOUR
T1 - Kinetic and Thermodynamic Aspects of Cellular Thiol-Disulfide Redox Regulation
AU - Jensen, Kristine Steen
AU - Hansen, Rosa Erritzøe
AU - Winther, Jakob R
PY - 2009
Y1 - 2009
N2 - Regulation of intracellular thiol-disulfide redox status is an essential part of cellular homeostasis. This involves the regulation of both oxidative and reductive pathways, production of oxidant scavengers and, importantly, the ability of cells to respond to changes in the redox environment. In the cytosol regulatory disulfide bonds are typically formed in spite of the prevailing reducing conditions and may thereby function as redox switches. Such disulfide bonds are protected from enzymatic reduction by kinetic barriers and are thus allowed to exist long enough to elicit the signal. Factors that affect the rate of thiol-disulfide exchange and stability of disulfide bonds are discussed within the framework of the underlying chemical foundations. This includes the effect of thiol acidity (pKa), the local electrostatic environment, molecular strain and entropy. Even though a thiol-disulfide exchange reaction is thermodynamically favourable it will only take place if the activation energy to form the transition state complex can be overcome. This is accomplished by enzymes, such as the oxidoreductases, that direct reactions in thermodynamically favourable directions by decreasing the activation energy barrier.
AB - Regulation of intracellular thiol-disulfide redox status is an essential part of cellular homeostasis. This involves the regulation of both oxidative and reductive pathways, production of oxidant scavengers and, importantly, the ability of cells to respond to changes in the redox environment. In the cytosol regulatory disulfide bonds are typically formed in spite of the prevailing reducing conditions and may thereby function as redox switches. Such disulfide bonds are protected from enzymatic reduction by kinetic barriers and are thus allowed to exist long enough to elicit the signal. Factors that affect the rate of thiol-disulfide exchange and stability of disulfide bonds are discussed within the framework of the underlying chemical foundations. This includes the effect of thiol acidity (pKa), the local electrostatic environment, molecular strain and entropy. Even though a thiol-disulfide exchange reaction is thermodynamically favourable it will only take place if the activation energy to form the transition state complex can be overcome. This is accomplished by enzymes, such as the oxidoreductases, that direct reactions in thermodynamically favourable directions by decreasing the activation energy barrier.
U2 - 10.1089/ARS.2008.2297
DO - 10.1089/ARS.2008.2297
M3 - Journal article
C2 - 19014315
VL - 11
SP - 1047
EP - 1058
JO - Antioxidants and Redox Signaling
JF - Antioxidants and Redox Signaling
SN - 1523-0864
IS - 5
ER -