Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/194681
Type: Artigo de periódico
Title: Sensitized Photooxygenation And Peroxidase-catalyzed Inactivation Of Xanthine Oxidase--evidence Of Cysteine Damage By Singlet Oxygen.
Author: Justo, G Z
Camargo, F A
Haun, M
Faljoni-Alário, A
Durán, N
Abstract: Xanthine oxidase (XO) has been investigated for its decreased activity in several cancerous tissues and constitutive generation of reactive oxygen species (ROS) in vivo seems to contribute significantly to its inactivation. Singlet oxygen (1O2) production has been suggested to be relevant when considering folic acid metabolism by cancer cells. Thus, the susceptibility of XO to inactivation by 1O2 generated either by the bioenergized systems folic acid/peroxidase/GSH/Mn2+/O2 and malonaldehyde/peroxidase/Mn2+/O2 or by methylene blue (MB) or eosin-sensitized photooxygenation was studied. Our results showed that other ROS were also responsible for XO inactivation when MB was used. In contrast, eosin produced almost exclusively 1O2. Kinetic studies of XO oxidation in the malonaldehyde/peroxidase system showed that histidine (His) is a competitive inhibitor with respect to XO. A similar result was observed in the eosin-photosensitized process, suggesting the involvement of 1O2 in both processes. In addition, an efficient quenching of XO oxidation by guanosine in the folic acid/peroxidase system was observed. Amino acid analysis revealed that cysteine (Cys) is more affected than other XO amino acids also prone to oxidation such as tyrosine (Tyr), methionine (Met) and His. These results indicate that 1O2 may cause oxidative damage to the Cys residues of XO, with loss of enzyme activity. Alteration of the flavin prosthetic site is hypothesized.
Subject: Amino Acids
Catalysis
Cysteine
Folic Acid
Glutathione
Horseradish Peroxidase
Indicators And Reagents
Malondialdehyde
Oxidation-reduction
Peroxidase
Photochemistry
Reactive Oxygen Species
Spectrometry, Fluorescence
Xanthine Oxidase
Citation: Physiological Chemistry And Physics And Medical Nmr. v. 32, n. 2, p. 145-54, 2000.
Rights: fechado
Address: http://www.ncbi.nlm.nih.gov/pubmed/11383136
Date Issue: 2000
Appears in Collections:Unicamp - Artigos e Outros Documentos

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