Photo-oxidation of proteins

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Photo-oxidation of proteins. / Pattison, David I; Rahmanto, Aldwin Suryo; Davies, Michael Jonathan.

In: Photochemical & Photobiological Sciences, Vol. 11, No. 1, 01.2012, p. 38-53.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Pattison, DI, Rahmanto, AS & Davies, MJ 2012, 'Photo-oxidation of proteins', Photochemical & Photobiological Sciences, vol. 11, no. 1, pp. 38-53. https://doi.org/10.1039/c1pp05164d

APA

Pattison, D. I., Rahmanto, A. S., & Davies, M. J. (2012). Photo-oxidation of proteins. Photochemical & Photobiological Sciences, 11(1), 38-53. https://doi.org/10.1039/c1pp05164d

Vancouver

Pattison DI, Rahmanto AS, Davies MJ. Photo-oxidation of proteins. Photochemical & Photobiological Sciences. 2012 Jan;11(1):38-53. https://doi.org/10.1039/c1pp05164d

Author

Pattison, David I ; Rahmanto, Aldwin Suryo ; Davies, Michael Jonathan. / Photo-oxidation of proteins. In: Photochemical & Photobiological Sciences. 2012 ; Vol. 11, No. 1. pp. 38-53.

Bibtex

@article{b2d691555e054a8a876b133da7d6eab9,
title = "Photo-oxidation of proteins",
abstract = "Photo-induced damage to proteins occurs via multiple pathways. Direct damage induced by UVB (λ 280-320 nm) and UVA radiation (λ 320-400 nm) is limited to a small number of amino acid residues, principally tryptophan (Trp), tyrosine (Tyr), histidine (His) and disulfide (cystine) residues, with this occurring via both excited state species and radicals. Indirect protein damage can occur via singlet oxygen ((1)O(2)(1)Δ(g)), with this resulting in damage to Trp, Tyr, His, cystine, cysteine (Cys) and methionine (Met) residues. Although initial damage is limited to these residues multiple secondary processes, that occur both during and after radiation exposure, can result in damage to other intra- and inter-molecular sites. Secondary damage can arise via radicals (e.g. Trp, Tyr and Cys radicals), from reactive intermediates generated by (1)O(2) (e.g. Trp, Tyr and His peroxides) and via molecular reactions of photo-products (e.g. reactive carbonyls). These processes can result in protein fragmentation, aggregation, altered physical and chemical properties (e.g. hydrophobicity and charge) and modulated biological turnover. Accumulating evidence implicates these events in cellular and tissue dysfunction (e.g. apoptosis, necrosis and altered cell signaling), and multiple human pathologies.",
keywords = "Disease, Humans, Oxidation-Reduction, Photochemistry, Proteins",
author = "Pattison, {David I} and Rahmanto, {Aldwin Suryo} and Davies, {Michael Jonathan}",
note = "This journal is {\circledC} The Royal Society of Chemistry and Owner Societies 2012",
year = "2012",
month = "1",
doi = "10.1039/c1pp05164d",
language = "English",
volume = "11",
pages = "38--53",
journal = "Photochemical & Photobiological Sciences",
issn = "1474-905X",
publisher = "Royal Society of Chemistry",
number = "1",

}

RIS

TY - JOUR

T1 - Photo-oxidation of proteins

AU - Pattison, David I

AU - Rahmanto, Aldwin Suryo

AU - Davies, Michael Jonathan

N1 - This journal is © The Royal Society of Chemistry and Owner Societies 2012

PY - 2012/1

Y1 - 2012/1

N2 - Photo-induced damage to proteins occurs via multiple pathways. Direct damage induced by UVB (λ 280-320 nm) and UVA radiation (λ 320-400 nm) is limited to a small number of amino acid residues, principally tryptophan (Trp), tyrosine (Tyr), histidine (His) and disulfide (cystine) residues, with this occurring via both excited state species and radicals. Indirect protein damage can occur via singlet oxygen ((1)O(2)(1)Δ(g)), with this resulting in damage to Trp, Tyr, His, cystine, cysteine (Cys) and methionine (Met) residues. Although initial damage is limited to these residues multiple secondary processes, that occur both during and after radiation exposure, can result in damage to other intra- and inter-molecular sites. Secondary damage can arise via radicals (e.g. Trp, Tyr and Cys radicals), from reactive intermediates generated by (1)O(2) (e.g. Trp, Tyr and His peroxides) and via molecular reactions of photo-products (e.g. reactive carbonyls). These processes can result in protein fragmentation, aggregation, altered physical and chemical properties (e.g. hydrophobicity and charge) and modulated biological turnover. Accumulating evidence implicates these events in cellular and tissue dysfunction (e.g. apoptosis, necrosis and altered cell signaling), and multiple human pathologies.

AB - Photo-induced damage to proteins occurs via multiple pathways. Direct damage induced by UVB (λ 280-320 nm) and UVA radiation (λ 320-400 nm) is limited to a small number of amino acid residues, principally tryptophan (Trp), tyrosine (Tyr), histidine (His) and disulfide (cystine) residues, with this occurring via both excited state species and radicals. Indirect protein damage can occur via singlet oxygen ((1)O(2)(1)Δ(g)), with this resulting in damage to Trp, Tyr, His, cystine, cysteine (Cys) and methionine (Met) residues. Although initial damage is limited to these residues multiple secondary processes, that occur both during and after radiation exposure, can result in damage to other intra- and inter-molecular sites. Secondary damage can arise via radicals (e.g. Trp, Tyr and Cys radicals), from reactive intermediates generated by (1)O(2) (e.g. Trp, Tyr and His peroxides) and via molecular reactions of photo-products (e.g. reactive carbonyls). These processes can result in protein fragmentation, aggregation, altered physical and chemical properties (e.g. hydrophobicity and charge) and modulated biological turnover. Accumulating evidence implicates these events in cellular and tissue dysfunction (e.g. apoptosis, necrosis and altered cell signaling), and multiple human pathologies.

KW - Disease

KW - Humans

KW - Oxidation-Reduction

KW - Photochemistry

KW - Proteins

U2 - 10.1039/c1pp05164d

DO - 10.1039/c1pp05164d

M3 - Journal article

C2 - 21858349

VL - 11

SP - 38

EP - 53

JO - Photochemical & Photobiological Sciences

JF - Photochemical & Photobiological Sciences

SN - 1474-905X

IS - 1

ER -

ID: 129669541