Singlet oxygen-mediated damage to proteins and its consequences

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Singlet oxygen-mediated damage to proteins and its consequences. / Davies, Michael Jonathan.

In: Molecular Cell Biology Research Communications, Vol. 305, No. 3, 06.06.2003, p. 761-70.

Research output: Contribution to journalJournal article

Harvard

Davies, MJ 2003, 'Singlet oxygen-mediated damage to proteins and its consequences', Molecular Cell Biology Research Communications, vol. 305, no. 3, pp. 761-70.

APA

Davies, M. J. (2003). Singlet oxygen-mediated damage to proteins and its consequences. Molecular Cell Biology Research Communications, 305(3), 761-70.

Vancouver

Davies MJ. Singlet oxygen-mediated damage to proteins and its consequences. Molecular Cell Biology Research Communications. 2003 Jun 6;305(3):761-70.

Author

Davies, Michael Jonathan. / Singlet oxygen-mediated damage to proteins and its consequences. In: Molecular Cell Biology Research Communications. 2003 ; Vol. 305, No. 3. pp. 761-70.

Bibtex

@article{3e716151f39c45de91d6206b5d6cde7d,
title = "Singlet oxygen-mediated damage to proteins and its consequences",
abstract = "Proteins comprise approximately 68{\%} of the dry weight of cells and tissues and are therefore potentially major targets for oxidative damage. Two major types of processes can occur during the exposure of proteins to UV or visible light. The first of these involves direct photo-oxidation arising from the absorption of UV radiation by the protein, or bound chromophore groups, thereby generating excited states (singlet or triplets) or radicals via photo-ionisation. The second major process involves indirect oxidation of the protein via the formation and subsequent reactions of singlet oxygen generated by the transfer of energy to ground state (triplet) molecular oxygen by either protein-bound, or other, chromophores. Singlet oxygen can also be generated by a range of other enzymatic and non-enzymatic reactions including processes mediated by heme proteins, lipoxygenases, and activated leukocytes, as well as radical termination reactions. This paper reviews the data available on singlet oxygen-mediated protein oxidation and concentrates primarily on the mechanisms by which this excited state species brings about changes to both the side-chains and backbone of amino acids, peptides, and proteins. Recent work on the identification of reactive peroxide intermediates formed on Tyr, His, and Trp residues is discussed. These peroxides may be important propagating species in protein oxidation as they can initiate further oxidation via both radical and non-radical reactions. Such processes can result in the transmittal of damage to other biological targets, and may play a significant role in bystander damage, or dark reactions, in systems where proteins are subjected to oxidation.",
keywords = "Humans, Light, Models, Chemical, Oxidative Stress, Proteins, Singlet Oxygen",
author = "Davies, {Michael Jonathan}",
year = "2003",
month = "6",
day = "6",
language = "English",
volume = "305",
pages = "761--70",
journal = "Molecular Cell Biology Research Communications",
issn = "1522-4724",
publisher = "Academic Press",
number = "3",

}

RIS

TY - JOUR

T1 - Singlet oxygen-mediated damage to proteins and its consequences

AU - Davies, Michael Jonathan

PY - 2003/6/6

Y1 - 2003/6/6

N2 - Proteins comprise approximately 68% of the dry weight of cells and tissues and are therefore potentially major targets for oxidative damage. Two major types of processes can occur during the exposure of proteins to UV or visible light. The first of these involves direct photo-oxidation arising from the absorption of UV radiation by the protein, or bound chromophore groups, thereby generating excited states (singlet or triplets) or radicals via photo-ionisation. The second major process involves indirect oxidation of the protein via the formation and subsequent reactions of singlet oxygen generated by the transfer of energy to ground state (triplet) molecular oxygen by either protein-bound, or other, chromophores. Singlet oxygen can also be generated by a range of other enzymatic and non-enzymatic reactions including processes mediated by heme proteins, lipoxygenases, and activated leukocytes, as well as radical termination reactions. This paper reviews the data available on singlet oxygen-mediated protein oxidation and concentrates primarily on the mechanisms by which this excited state species brings about changes to both the side-chains and backbone of amino acids, peptides, and proteins. Recent work on the identification of reactive peroxide intermediates formed on Tyr, His, and Trp residues is discussed. These peroxides may be important propagating species in protein oxidation as they can initiate further oxidation via both radical and non-radical reactions. Such processes can result in the transmittal of damage to other biological targets, and may play a significant role in bystander damage, or dark reactions, in systems where proteins are subjected to oxidation.

AB - Proteins comprise approximately 68% of the dry weight of cells and tissues and are therefore potentially major targets for oxidative damage. Two major types of processes can occur during the exposure of proteins to UV or visible light. The first of these involves direct photo-oxidation arising from the absorption of UV radiation by the protein, or bound chromophore groups, thereby generating excited states (singlet or triplets) or radicals via photo-ionisation. The second major process involves indirect oxidation of the protein via the formation and subsequent reactions of singlet oxygen generated by the transfer of energy to ground state (triplet) molecular oxygen by either protein-bound, or other, chromophores. Singlet oxygen can also be generated by a range of other enzymatic and non-enzymatic reactions including processes mediated by heme proteins, lipoxygenases, and activated leukocytes, as well as radical termination reactions. This paper reviews the data available on singlet oxygen-mediated protein oxidation and concentrates primarily on the mechanisms by which this excited state species brings about changes to both the side-chains and backbone of amino acids, peptides, and proteins. Recent work on the identification of reactive peroxide intermediates formed on Tyr, His, and Trp residues is discussed. These peroxides may be important propagating species in protein oxidation as they can initiate further oxidation via both radical and non-radical reactions. Such processes can result in the transmittal of damage to other biological targets, and may play a significant role in bystander damage, or dark reactions, in systems where proteins are subjected to oxidation.

KW - Humans

KW - Light

KW - Models, Chemical

KW - Oxidative Stress

KW - Proteins

KW - Singlet Oxygen

M3 - Journal article

C2 - 12763058

VL - 305

SP - 761

EP - 770

JO - Molecular Cell Biology Research Communications

JF - Molecular Cell Biology Research Communications

SN - 1522-4724

IS - 3

ER -

ID: 138275833