Abstract
Protein modifications, such as carbonylation, nitration and formation of lipid peroxidation adducts, e.g. 4-hydroxynonenal (HNE), are products of oxidative damage attributed to reactive oxygen species (ROS). The mitochondrial respiratory chain Complexes I and III have been shown to be a major source of ROS in vitro. Additionally, modifications of the respiratory chain Complexes (I-V) by nitration, carbonylation and HNE adduct decrease their enzymatic activity in vitro. However, modification of these respiratory chain complex proteins due to in vivo basal level ROS generation has not been investigated. In this study, we show a basal level of oxidative damage to specific proteins of adult bovine heart submitochondrial particle (SMP) complexes, and find that most of these proteins are localized in the mitochondrial matrix. We postulate that electron leakage from respiratory chain complexes and subsequent ROS formation may cause damage to specific complex subunits and contribute to long-term accumulation of mitochondrial dysfunction.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 95-101 |
| Number of pages | 7 |
| Journal | Biochimica et Biophysica Acta - Molecular Basis of Disease |
| Volume | 1688 |
| Issue number | 2 |
| DOIs | |
| State | Published - Mar 2 2004 |
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Keywords
- 4-hydroxynonenal
- Carbonylation
- Lipid peroxidation adduct
- Mitochondrial dysfunction
- Nitration
- Oxidative stress
ASJC Scopus subject areas
- Molecular Biology
- Molecular Medicine
- Biophysics
Cite this
Oxidatively damaged proteins of heart mitochondrial electron transport complexes. / Choksi, K. B.; Boylston, W. H.; Rabek, J. P.; Widger, W. R.; Papaconstantinou, John.
In: Biochimica et Biophysica Acta - Molecular Basis of Disease, Vol. 1688, No. 2, 02.03.2004, p. 95-101.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Oxidatively damaged proteins of heart mitochondrial electron transport complexes
AU - Choksi, K. B.
AU - Boylston, W. H.
AU - Rabek, J. P.
AU - Widger, W. R.
AU - Papaconstantinou, John
PY - 2004/3/2
Y1 - 2004/3/2
N2 - Protein modifications, such as carbonylation, nitration and formation of lipid peroxidation adducts, e.g. 4-hydroxynonenal (HNE), are products of oxidative damage attributed to reactive oxygen species (ROS). The mitochondrial respiratory chain Complexes I and III have been shown to be a major source of ROS in vitro. Additionally, modifications of the respiratory chain Complexes (I-V) by nitration, carbonylation and HNE adduct decrease their enzymatic activity in vitro. However, modification of these respiratory chain complex proteins due to in vivo basal level ROS generation has not been investigated. In this study, we show a basal level of oxidative damage to specific proteins of adult bovine heart submitochondrial particle (SMP) complexes, and find that most of these proteins are localized in the mitochondrial matrix. We postulate that electron leakage from respiratory chain complexes and subsequent ROS formation may cause damage to specific complex subunits and contribute to long-term accumulation of mitochondrial dysfunction.
AB - Protein modifications, such as carbonylation, nitration and formation of lipid peroxidation adducts, e.g. 4-hydroxynonenal (HNE), are products of oxidative damage attributed to reactive oxygen species (ROS). The mitochondrial respiratory chain Complexes I and III have been shown to be a major source of ROS in vitro. Additionally, modifications of the respiratory chain Complexes (I-V) by nitration, carbonylation and HNE adduct decrease their enzymatic activity in vitro. However, modification of these respiratory chain complex proteins due to in vivo basal level ROS generation has not been investigated. In this study, we show a basal level of oxidative damage to specific proteins of adult bovine heart submitochondrial particle (SMP) complexes, and find that most of these proteins are localized in the mitochondrial matrix. We postulate that electron leakage from respiratory chain complexes and subsequent ROS formation may cause damage to specific complex subunits and contribute to long-term accumulation of mitochondrial dysfunction.
KW - 4-hydroxynonenal
KW - Carbonylation
KW - Lipid peroxidation adduct
KW - Mitochondrial dysfunction
KW - Nitration
KW - Oxidative stress
UR - http://www.scopus.com/inward/record.url?scp=1342264360&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=1342264360&partnerID=8YFLogxK
U2 - 10.1016/j.bbadis.2003.11.007
DO - 10.1016/j.bbadis.2003.11.007
M3 - Article
C2 - 14990339
AN - SCOPUS:1342264360
VL - 1688
SP - 95
EP - 101
JO - Biochimica et Biophysica Acta - Molecular Basis of Disease
JF - Biochimica et Biophysica Acta - Molecular Basis of Disease
SN - 0925-4439
IS - 2
ER -