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Browsing by Author "Fuentes Lemus, Eduardo Felipe"

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Aggregation of alpha- and beta- caseins induced by peroxyl radicals involves secondary reactions of carbonyl compounds as well as di-tyrosine and di-tryptophan formation
(2018) Fuentes Lemus, Eduardo Felipe; Silva, Eduardo; Barrias, Pablo; Aspee, Alexis; Escobar Álvarez, Elizabeth; Lorentzen, Lasse G.; Carroll, Luke; Leinisch, Fabian; Davies, Michael J.; López Alarcón, Camilo Ignacio
Alpha- and beta-casein aggregation induced by riboflavin-sensitized photo-oxidation occurs via di-tyrosine cross-links and is oxygen concentration dependent
(2018) Fuentes Lemus, Eduardo Felipe; Silva, E.; Leinisch, F.; Dorta Pérez, Eva; Lorentzen, L. G.; Davies, M. J.; López Alarcón, Camilo Ignacio
Azocompounds as generators of defined radical species: Contributions and challenges for free radical research
(2020) López Alarcón, Camilo Ignacio; Fuentes Lemus, Eduardo Felipe; Figueroa Alegría, Juan David; Dorta, Eva; Schöneich, Christian; Davies, Michael J.
Peroxyl radicals participate in multiple processes involved in critical changes to cells, tissues, pharmacueticals and foods. Some of these reactions explain their association with degenerative pathologies, including cardiovascular and neurological diseases, as well as cancer development. Azocompounds, and particularly AAPH (2,2 ' Azobis(2-methylpropionamidine) dihydrochloride), a cationic water-soluble derivative, have been employed extensively as sources of model peroxyl radicals. A considerable number of studies have reported mechanistic data on the oxidation of biologically-relevant targets, the scavenging activity of foods and natural products, and the reactions with, and responses of, cultured cells. However, despite the (supposed) experimental simplicity of using azocompounds, the chemistry of peroxyl radical production and subsequent reactions is complicated, and not always considered in sufficient depth when analyzing experimental data. The present work discusses the chemical aspects of azocompounds as generators of peroxyl (and other) radicals, together with their contribution to our understanding of biochemistry, pharmaceutical and food chemistry research. The evidence supporting a role for the formation of alkoxyl (RO center dot) and other radicals during thermal and photochemical decomposition of azocompounds is assessed, together with the potential influence of such species on the reactions under study.
Binding of rose bengal to lysozyme modulates photooxidation and cross-linking reactions involving tyrosine and tryptophan
(2019) Fuentes Lemus, Eduardo Felipe; Mariotti, Michele; Hägglund, Per; Leinisch, Fabian; Fierro Huerta, Angélica; Silva, Eduardo; López Alarcón, Camilo Ignacio; Davies, Michael J.
Complexes between 2,20-azobis(2methylpropionamidine) dihydrochloride (AAPH) and cucurbit[n]uril hosts modulate the yield and fate of photolytically-generated AAPH radicals
(Royal Society of Chemistry, 2024) Forero Girón, Angie; Oyarzún Alfaro, Mauricio Sebastián; Droguett Muñoz, Kevin Arturo; Fuentealba Patiño, Denis Alberto; Gutiérrez Oliva, Soledad; Herrera Pisani, Bárbara Andrea; Toro Labbé, Alejandro; Fuentes Lemus, Eduardo Felipe; Davies, Michael J.; López Alarcón, Camilo Ignacio; Aliaga Miranda, Margarita Elly
Using theoretical and experimental tools we investigated the recognition of AAPH (2,2′-azobis(2-methylpropionamidine) dihydrochloride), a well-known water-soluble azo-compound employed as a source of peroxyl radicals, by cucurbit[6]uril (CB[6]), and cucurbit[8]uril (CB[8]). Density functional theory calculations and isothermal titration calorimetry experiments demonstrated that AAPH was not included in the cavity of CB[6], however, an exclusion complex was generated. Inclusion of AAPH in the CB[8] cavity was favored, forming stable inclusion complexes at 1 : 1 and 2 : 1 stoichiometries; AAPH@CB[8] and 2AAPH@CB[8], respectively. Radical formation upon photolytic cleavage of AAPH was examined theoretically, and by spin trapping with electron paramagnetic resonance. The radical yields detected with uncomplexed (free) AAPH and the AAPH-CB[6] (exclusion) complex were identical, whereas a marked decrease was shown for AAPH@CB[8]. Lower decreases were seen with a bimolecular (2 : 1) AAPH-CB[8] inclusion complex (2AAPH@CB[8]). This modulation was corroborated by the consumption of pyrogallol red (PGR), an oxidizable dye that does not associate with CB[6] or CB[8]. AAPH-CB[6] and 2AAPH@CB[8] did not significantly modify the initial consumption rate (Ri) of PGR, whereas AAPH@CB[8] decreased this. The oxidative consumption of free Trp, Gly-Trp and Trp-Gly by radicals derived from AAPH in the presence of CB[8] showed a dependence on the association of the targets with CB[8].
Crowding modulates the glycation of plasma proteins: In vitro analysis of structural modifications to albumin and transferrin and identification of sites of modification
(2022) Fuentes Lemus, Eduardo Felipe; Reyes Valenzuela, Juan Sebastián; López Alarcón, Camilo Ignacio; Davies, Michael J.
Protein modification occurs in biological milieus that are characterized by high concentrations of (macro)mol-ecules (i.e. heterogeneous and packed environments). Recent data indicate that crowding can modulate the extent and rate of protein oxidation, however its effect on other post-translational modifications remains to be explored. In this work we hypothesized that crowding would affect the glycation of plasma proteins. Physiologically-relevant concentrations of albumin (35 mg mL-1) and transferrin (2 mg mL-1) were incubated with methylglyoxal and glyoxal (5 mu M-5 mM), two alpha-oxoaldehyde metabolites that are elevated in the plasma of people with diabetes. Crowding was induced by adding dextran or ficoll polymers. Electrophoresis, electron microscopy, fluorescence spectroscopy and mass spectrometry were employed to investigate the structural consequences of glycation under crowded conditions. Our data demonstrate that crowding modulates the extent of formation of transferrin cross-links, and also the modification pathways in both albumin and transferrin. Arginine was the most susceptible residue to modification, with lysine and cysteine also affected. Loss of 0.48 and 7.28 arginine residues per protein molecule were determined on incubation with 500 mu M methylglyoxal for albumin and transferrin, respectively. Crowding did not influence the extent of loss of arginine and lysine for either protein, but the sites of modification, detected by LC-MS, were different between dilute and crowded conditions. These data confirm the relevance of studying modification processes under conditions that closely mimic biological milieus. These data unveil additional factors that influence the pattern and extent of protein modification, and their structural consequences, in biological systems.
Effect of macromolecular crowding on protein oxidation: Consequences on the rate, extent and oxidation pathways
(2021) Fuentes Lemus, Eduardo Felipe; Reyes Valenzuela, Juan Sebastián; Gamon, Luke F.; López Alarcón, Camilo Ignacio; Davies, Michael J.
Biological systems are heterogeneous and crowded environments. Such packed milieus are expected to modulate reactions both inside and outside the cell, including protein oxidation. In this work, we explored the effect of macromolecular crowding on the rate and extent of oxidation of Trp and Tyr, in free amino acids, peptides and proteins. These species were chosen as they are readily oxidized and contribute to damage propagation. Dextran was employed as an inert crowding agent, as this polymer decreases the fraction of volume available to other (macro)molecules. Kinetic analysis demonstrated that dextran enhanced the rate of oxidation of free Trp, and peptide Trp, elicited by AAPH-derived peroxyl radicals. For free Trp, the rates of oxidation were 15.0 ± 2.1 and 30.5 ± 3.4 μM min−1 without and with dextran (60 mg mL−1) respectively. Significant increases were also detected for peptide-incorporated Trp. Dextran increased the extent of Trp consumption (up to 2-fold) and induced short chain reactions. In contrast, Tyr oxidation was not affected by the presence of dextran. Studies on proteins, using SDS-PAGE and LC-MS, indicated that oxidation was also affected by crowding, with enhanced amino acid loss (45% for casein), chain reactions and altered extents of oligomer formation. The overall effects of dextran-mediated crowding were however dependent on the protein structure. Overall, these data indicate that molecular crowding, as commonly encountered in biological systems affect the rates, and extents of oxidation, and particularly of Trp residues, illustrating the importance of appropriate choice of in vitro systems to study biological oxidations.
Enzymes of glycolysis and the pentose phosphate pathway as targets of oxidants: Role of redox reactions on the carbohydrate catabolism
(2025) Fuentes Lemus, Eduardo Felipe; Usgame Fagua, Karen Gineth; Fierro Huerta, Angelica María; López Alarcón, Camilo Ignacio
Redox reactions can modulate metabolic and signaling pathways with consequences on cellular adaptation to different stimuli. The abundance and structural features of some metabolic enzymes make these targets of oxidants, including one- and two-electron oxidant molecules, altering their structure and/or function. Therefore, redox processes play an important role in physiology and pathology. In particular, the oxidative post- translational modification of the enzymes that participate in glycolysis and the pentose phosphate pathway (PPP) can modulate the carbon flux affecting synthesis of nucleotides, as well as production of adenosine triphosphate (ATP) and reducing equivalents (in the form of nicotinamide adenine dinucleotide phosphate, NADPH). Specifically, generation of NADPH, a cofactor important for cell homeostasis, is key to the management of the redox status of cells towards oxidative insults. In this review we discuss the available literature on the impact of oxidative post-translational modifications on key glycolytic and PPP enzymes with an analysis of the consequences these may have for cell metabolic adaptation. We also discuss the contributions of new experimental and in silico approaches to the redox biochemistry field, which have significantly illuminated the intricate relationship between the pathways involved in carbohydrate metabolism and how these could be regulated by redox reactions.
Evaluation of the antioxidant capacity of food samples: a chemical examination of the oxygen radical absorbance capacity assay
(WILEY-BLACKWELL, 2018) Dorta Pérez, Eva; Fuentes Lemus, Eduardo Felipe; Speisky, Hernan; Lissi Gervaso, Eduardo A.; López Alarcón, Camilo Ignacio; Apak, Resat; Capanoglu, Esra; Shahidi, Fereidoon
This chapter describes, from a critical point of view, the main in vitro methodologies employed to assess the antioxidant capacity (AC) of food samples. Considering the wide use of the oxygen radical absorbance capacity (ORAC) assay, it presents a chemical examination of this methodology. The methods for AC evaluation are based on different strategies; these include the use of colored and stable free radicals, evaluation of the capacity of antioxidants to reduce cupric or ferric ions, estimation of the ability of phenolic compounds (PC) to protect a target molecule exposed to a free radical source, and evaluation of the capacity of PC to form nanoparticles. When the antioxidant activity of a particular sample is evaluated, it is recommended to know the meanings and limitations of the assays being employed. In the case of the ORAC assay, the nature of the free radicals generated during the thermolysis of AAPH should also be considered.
Formation and characterization of crosslinks, including Tyr-Trp species, on one electron oxidation of free Tyr and Trp residues by carbonate radical anion
(2020) Figueroa Alegría, Juan David; Zarate Méndez, Ana María; Fuentes Lemus, Eduardo Felipe; Davies, M. J.; Lopez Alarcon Camilo Ignacio
Dityrosine and ditryptophan bonds have been implied in protein crosslinking. This is associated with oxidative stress conditions including those involved in neurodegenerative pathologies and age-related processes. Formation of dityrosine and ditryptophan derives from radical-radical reactions involving Tyr(center dot) and Trp(center dot) radicals. However, cross reactions of Tyr(center dot) and Trp(center dot) leading to Tyr-Trp crosslinks and their biological consequences have been less explored. In the present work we hypothesized that exposure of free Tyr and Trp to a high concentration of carbonate anion radicals (CO3 center dot-), under anaerobic conditions, would result in the formation of Tyr-Trp species, as well as dityrosine and ditryptophan crosslinks. Here we report a simple experimental procedure, employing CO3 center dot- generated photochemically by illumination of a Co(iii) complex at 254 nm, that produces micromolar concentrations of Tyr-Trp crosslinks. Analysis by mass spectrometry of solutions containing only the individual amino acids, and the Co(iii) complex, provided evidence for the formation ofo,o '-dityrosine and isodityrosine from Tyr, and three ditryptophan dimers from Trp. When mixtures of Tyr and Trp were illuminated in an identical manner, Tyr-Trp crosslinks were detected together with dityrosine and ditryptophan dimers. These results indicate that there is a balance between the formation of these three classes of crosslinks, which is dependent on the Tyr and Trp concentrations. The methods reported here allow the generation of significant yields of isolated Tyr-Trp adducts and their characterization. This technology should facilitate the detection, and examination of the biological consequences of Tyr-Trp crosslink formation in complex systems in future investigations.
Free radicals derived from gamma-radiolysis of water and AAPH thermolysis mediate oxidative crosslinking of eGFP involving Tyr-Tyr and Tyr-Cys bonds : the fluorescence of the protein is conserved only towards peroxyl radicals
(2020) Zamora Jofré, Renato Andrés; Fuentes Lemus, Eduardo Felipe; Barrias, P.; Herrera-Morande, A.; Mura, F.; Guixe, V.; Castro-Fernandez, V.; Rojas, T.; López Alarcón, Camilo Ignacio; Aguirre, P.; Rivas-Aravena, A.; Aspee, A.
Implications of differential peroxyl radical-induced inactivation of glucose 6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase for the pentose phosphate pathway
(Nature Research, 2022) Reyes Valenzuela, Juan Sebastián; Figueroa Alegría, Juan David; Martínez Rojas, Francisco Javier; López Alarcon, Camilo Ignacio; Fuentes Lemus, Eduardo Felipe; Hagglund, P.M.; Davies, Michael J.; Fierro Huerta, Angelica María; Arenas, Felipe
© 2022, The Author(s).Escherichia coli glucose-6-phosphate dehydrogenase (G6PDH) and 6-phosphogluconate dehydrogenase (6PGDH) are key enzymes of the pentose phosphate pathway, responsible for the NADPH production in cells. We investigated modification of both enzymes mediated by peroxyl radicals (ROO·) to determine their respective susceptibilities to and mechanisms of oxidation. G6PDH and 6PGDH were incubated with AAPH (2,2?-azobis(2-methylpropionamidine)dihydrochloride), which was employed as ROO· source. The enzymatic activities of both enzymes were determined by NADPH release, with oxidative modifications examined by electrophoresis and liquid chromatography (LC) with fluorescence and mass (MS) detection. The activity of G6PDH decreased up to 62.0 ± 15.0% after 180 min incubation with 100 mM AAPH, whilst almost total inactivation of 6PGDH was determined under the same conditions. Although both proteins contain abundant Tyr (particularly 6PGDH), these residues were minimally affected by ROO·, with Trp and Met being major targets. LC–MS and in silico analysis showed that the modification sites of G6PDH are distant to the active site, consistent with a dispersed distribution of modifications, and inactivation resulting from oxidation of multiple Trp and Met residues. In contrast, the sites of oxidation detected on 6PGDH are located close to its catalytic site indicating a more localized oxidation, and a consequent high susceptibility to ROO·-mediated inactivation.
Oxidación de caseínas inducida por radicales peroxilo y procesos fotoquímicos sensibilizados por riboflavina
(2018) Fuentes Lemus, Eduardo Felipe; López Alarcón, Camilo Ignacio; Pontificia Universidad Católica de Chile. Facultad de Química
En la leche entera, la coexistencia de la riboflavina (RF, vitamina B2), los lípidos y las proteínas constituye un escenario favorable para los procesos de oxidación. En particular la exposición a la luz visible u otros factores conducen la generación del estado excitado triplete de la RF (3RF) y de los radicales peroxilo (ROO•). Ambas especies son capaces de inducir la oxidación de las caseínas (las principales proteínas lácteas) mediante reacciones que no solo llevan a la oxidación de la cadena lateral de aminoácidos (Trp, Tyr, Met, e His) sino que también pueden derivar en el entrecruzamiento y/o la fragmentación proteica. La etiología de éstas modificaciones es de actual investigación, en especial el entrecruzamiento mediado por reacciones radical-radical que lleva a la formación de enlaces diTrp. Se espera que este tipo de reacciones estén favorecidas por la elevada flexibilidad de las caseínas, siendo la fuente oxidativa, la dosis de radicales libres y los aminoácidos involucrados determinantes en las modificaciones oxidativas. Para dilucidar estos aspectos, en la presente tesis se estudiaron los cambios en la estructura y composición de la α- y la β-caseína inducidos por el 3RF y los ROO• (generados por la termólisis de AAPH (2,2'-azobis (2-metilpropionamidina) dihidrocloruro). Las muestras fueron analizadas mediante electroforesis, inmunoblot, fluorescencia y cromatografía líquida. La exposición de las caseínas al AAPH y procesos sensibilizados por el 3RF dio como resultado un extenso consumo de monómeros y altos niveles de agregación proteica. El Trp y la Tyr fueron consumidos eficientemente, con niveles de diTyr y diTrp dependientes de la naturaleza del oxidante y la presencia del O2. El entrecruzamiento de las caseínas sensibilizado por el 3RF fue exclusivamente asociado a diTyr ydiTrp bajo una atmósfera de N2. En presencia del O2 rutas alternativas de entrecruzamiento fueron evidenciadas. En contraste, con los ROO•, el principal mecanismo de entrecruzamiento fue la reacción de los grupos carbonilo con los residuos de Lys.
Oxidation of free, peptide and protein tryptophan residues mediated by AAPH-derived free radicals: role of alkoxyl and peroxyl radicals
(2016) Fuentes Lemus, Eduardo Felipe; Dorta Pérez, Eva; Escobar Álvarez, Elizabeth; Aspée, A.; Pino, E.; Abasq, M. L.; Speisky, Hernán; Silva, E.; Lissi, E.; Davies, M. J.; López Alarcón, Camilo Ignacio
Oxidation of lysozyme induced by peroxyl radicals involves amino acid modifications, loss of activity, and formation of specific crosslinks
(2021) Fuentes Lemus, Eduardo Felipe; Mariotti, Michele; Hägglund, Per; Leinisch, Fabian; Fierro Huerta, Angélica; Silva Stevens, Eduardo Andrés; Davies, Michael J.; López Alarcón, Camilo Ignacio
The present work examined the oxidation and crosslinking of the anti-bacterial enzyme lysozyme (Lyso), which is present in multiple biological fluids, and released from the cytoplasmic granules of macrophages and neutrophils at sites of infection and inflammation. It is therefore widely exposed to oxidants including peroxyl radicals (ROO?). We hypothesized that exposure to ROO? would generate specific modifications and inter- and intraprotein crosslinks via radical-radical reactions. Lyso was incubated with AAPH (2,2?-azobis(2-methylpropionamidine) dihydrochloride) as a ROO? source. Enzymatic activity was assessed, while oxidative modifications were detected and quantified using electrophoresis and liquid chromatography (UPLC) with fluorescence or mass detection (MS). Computational models of AAPH-Lyso interactions were developed. Exposure of Lyso to AAPH (10 and 100 mM for 3 h, and 20 mM for 1 h), at 37 ?C, decreased enzymatic activity. 20 mM AAPH showed the highest efficiency of Lyso inactivation (1.78 mol of Lyso inactivated per ROO?). Conversion of Met to its sulfoxide, and to a lesser extent, Tyr oxidation to 3,4-dihydroxyphenylalanine and diTyr, were detected by UPLCMS. Extensive transformation of Trp, involving short chain reactions, to kynurenine, oxindole, hydroxytryptophan, hydroperoxides or di-alcohols, and N-formyl-kynurenine was detected, with Trp62, Trp63 and Trp108 the most affected residues. Interactions of AAPH inside the negatively-charged catalytic pocket of Lyso, with Trp108, Asp52, and Glu35, suggest that Trp108 oxidation mediates, at least partly, Lyso inactivation. Crosslinks between Tyr20-Tyr23 (intra-molecular), and Trp62-Tyr23 (inter-molecular), were detected with both proximity (Tyr20-Tyr23), and chain flexibility (Trp62) appearing to favor the formation of covalent crosslinks.
Oxidation of myofibrillar proteins induced by peroxyl radicals : role of oxidizable amino acids
(2019) Dorta Pérez, Eva; Avila, F.; Fuentes Lemus, Eduardo Felipe; Fuentealba Patiño, Denis Alberto; López Alarcón, Camilo Ignacio
Oxidative Crosslinking of Peptides and Proteins: Mechanisms of Formation, Detection, Characterization and Quantification
(2022) Fuentes Lemus, Eduardo Felipe; Hägglund, Per; López Alarcón, Camilo Ignacio; Davies, Michael J.
Covalent crosslinks within or between proteins play a key role in determining the structure and function of proteins. Some of these are formed intentionally by either enzymatic or molecular reactions and are critical to normal physiological function. Others are generated as a consequence of exposure to oxidants (radicals, excited states or two-electron species) and other endogenous or external stimuli, or as a result of the actions of a number of enzymes (e.g., oxidases and peroxidases). Increasing evidence indicates that the accumulation of unwanted crosslinks, as is seen in ageing and multiple pathologies, has adverse effects on biological function. In this article, we review the spectrum of crosslinks, both reducible and non-reducible, currently known to be formed on proteins; the mechanisms of their formation; and experimental approaches to the detection, identification and characterization of these species.
Peroxyl radicals modify 6-phosphogluconolactonase from Escherichia coli via oxidation of specific amino acids and aggregation which inhibits enzyme activity
(ELSEVIER SCIENCE INC, 2023) Reyes Valenzuela, Juan Sebastián; Fuentes Lemus, Eduardo Felipe; Romero, Jefferson; Arenas, Felipe; Fierro Huerta, Angelica María; Davies, Michael J.; Lopez Alarcon Camilo Ignacio
6-phosphogluconolactonase (6PGL) catalyzes the second reaction of the pentose phosphate pathway (PPP) converting 6-phosphogluconolactone to 6-phosphogluconate. The PPP is critical to the generation of NADPH and metabolic intermediates, but some of its components are susceptible to oxidative inactivation. Previous studies have characterized damage to the first (glucose-6-phosphate dehydrogenase) and third (6-phosphogluconate dehydrogenase) enzymes of the pathway, but no data are available for 6PGL. This knowledge gap is addressed here. Oxidation of Escherichia coli 6PGL by peroxyl radicals (ROO center dot, from AAPH (2,2 '-azobis(2-methylpropionamidine) dihydrochloride) was examined using SDS-PAGE, amino acid consumption, liquid chromatography with mass detection (LC-MS), protein carbonyl formation and computational methods. NADPH generation was assessed using mixtures all three enzymes of the oxidative phase of the PPP. Incubation of 6PGL with 10 or 100 mM AAPH resulted in protein aggregation mostly due to reducible (disulfide) bonds. High fluxes of ROO center dot induced consumption of Cys, Met and Trp, with the Cys oxidation rationalizing the aggregate formation. Low levels of carbonyls were detected, while LC-MS analyses provided evidence for oxidation of selected Trp and Met residues (Met1, Trp18, Met41, Trp203, Met220 and Met221). ROO center dot elicited little loss of enzymatic activity of monomeric 6PGL, but the aggregates showed diminished NADPH generation. This is consistent with in silico analyses that indicate that the modified Trp and Met are far from the 6-phosphogluconolactone binding site and the catalytic dyad (His130 and Arg179). Together these data indicate that monomeric 6PGL is a robust enzyme towards oxidative inactivation by ROO center dot and when compared to other PPP enzymes.
Photo -oxidation of lysozyme triggered by riboflavin is O 2-dependent, occurs via mixed type 1 and type 2 pathways, and results in inactivation, site-specific damage and intra- and inter -molecular crosslinks
(2020) Fuentes Lemus, Eduardo Felipe; Mariotti, M.; Reyes Martinez, Juan; Leinisch, F.; Hagglund, P.; Silva, E.; Davies, M. J.; López Alarcón, Camilo Ignacio
Photo-induced protein oxidation: mechanisms, consequences and medical applications
(2020) Fuentes Lemus, Eduardo Felipe; López Alarcón, Camilo Ignacio
Irradiation from the sun has played a crucial role in the origin and evolution of life on the earth. Due to the presence of ozone in the stratosphere most of the hazardous irradiation is absorbed, nonetheless UVB, UVA, and visible light reach the earth's surface. The high abundance of proteins in most living organisms, and the presence of chromophores in the side chains of certain amino acids, explain why these macromolecules are principal targets when biological systems are illuminated. Light absorption triggers the formation of excited species that can initiate photo-modification of proteins. The major pathways involve modifications derived from direct irradiation and photo-sensitized reactions. In this review we explored the basic concepts behind these photochemical pathways, with special emphasis on the photosensitized mechanisms (type 1 and type 2) leading to protein oxidation, and how this affects protein structure and functions. Finally, a description of the photochemical reactions involved in some human diseases, and medical applications of protein oxidation are presented.

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