Amino acids and proteins in photochemistry
(2007) L’actualité Chimique — n° 308-309, p. 15-18 (2007)
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- Abstract
- Photooxidation of proteins may result from a direct reactivity of the amino acids such as tyrosin or tryptophane with UV radiation. Recent data highlight the major role of the dissociative states of protonated aromatic amino acids in photofragmentation. This process can result from the loss of a hydrogen atom with formation of a radical cation. This will be a powerful tool to cleave selectively peptides. Proteins as DNA may also be the target of photosensitizers such as polyazaaromatic Ru-11 complexes. An important property of these compounds with very oxidative ligands is their very high oxidation power in the (MLCT)-M-3 (metal-to-ligand charge transfer) state. At the excited state, they are able to abstract an electron from electron donors such as the tryptophane. This reactivity can give rise to the formation of covalent photoadducts with the tryptophane. The formation of such damage displays a potent interest for the photodynamic therapy. Moreover, complex electron transfer reactions may also occur between ruthenium compounds under illumination and a metallo-protein such the superoxyde dismutase Cu/Zn leading to an inhibition of the enzymatic activity.
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Vicendo, P., Bijeire, L., Elias, B., Jouvet, C., Kirsch-De Mesmaeker, A., & Moucheron, C. (2007). Amino acids and proteins in photochemistry. L’actualité Chimique, 308-309, 15-18. https://hdl.handle.net/2078.5/51849 (Original work published 2007)