Redox Biochemistry and Chemistry最新文献_第2页

Near UV and visible light photo-degradation of therapeutic proteins: reaction mechanisms and significance for the development of pharmaceutical formulations 近紫外和可见光下治疗性蛋白质的降解：反应机制及其对药物配方开发的意义

Redox Biochemistry and Chemistry Pub Date : 2025-12-01 Epub Date: 2025-10-31 DOI: 10.1016/j.rbc.2025.100065

Christian Schöneich

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Oxidized phospholipids in ferroptosis, immunity and inflammation 氧化磷脂在铁下垂、免疫和炎症中的作用

Redox Biochemistry and Chemistry Pub Date : 2025-12-01 Epub Date: 2025-10-09 DOI: 10.1016/j.rbc.2025.100061

Valerie B. O'Donnell , Valery Bochkov

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Photosensitized oxidative crosslinking of bovine serum albumin and the impact on its esterase-like activity 牛血清白蛋白光敏氧化交联及其对酯酶样活性的影响

Redox Biochemistry and Chemistry Pub Date : 2025-12-01 Epub Date: 2025-09-12 DOI: 10.1016/j.rbc.2025.100060

Claudia Cecilia Vera , Jesús M.N. Morales , María del Pilar Guauque Torres , Mariana P. Serrano , Claudio D. Borsarelli

{"title":"Photosensitized oxidative crosslinking of bovine serum albumin and the impact on its esterase-like activity","authors":"Claudia Cecilia Vera , Jesús M.N. Morales , María del Pilar Guauque Torres , Mariana P. Serrano , Claudio D. Borsarelli","doi":"10.1016/j.rbc.2025.100060","DOIUrl":"10.1016/j.rbc.2025.100060","url":null,"abstract":"<div><div>A photosensitized oxidative crosslinking of proteins (POCP) reaction was applied in air-saturated phosphate buffer solutions of bovine serum albumin (BSA) to obtain soluble protein nanoparticles of approximately 100 nm in diameter. A royal blue LED was used as the excitation source for the photosensitizer molecule ruthenium (II) tris(2,2′-bipyridyl) dication (Ru(bpy)<sub>3</sub><sup>2+</sup>), in the presence of the electron acceptor persulfate anion (S<sub>2</sub>O<sub>8</sub><sup>2−</sup>). The redox quenching products prompted the formation of side-chain tyrosyl radicals, which served as intermediaries in the covalent attachment between proteins, leading to the formation of dityrosine (Tyr<sub>2</sub>) links. However, the dissolved oxygen competes efficiently with S<sub>2</sub>O<sub>8</sub><sup>2−</sup> to quench the excited photosensitizer, thereby generating singlet molecular oxygen (<sup>1</sup>O<sub>2</sub>), which reacts with electron-rich protein residues, which in turn induce an additional oxidative pattern of BSA. Consequently, under air-saturated conditions, the POCP gives rise to a series of oxygen-dependent and -independent reactions, resulting in the protein crosslinking with oxidative modifications. The esterase-like activity efficacy of BSA oxidized solely by <sup>1</sup>O<sub>2</sub> and after the formation of oligomeric protein nanoparticles by POCP was reduced by 51 % and 73 %, respectively, as compared with that of the native BSA. The combination of the oxidative degradation of key residues in the active sites and steric impediment due to protein oligomerization was found to be associated with this result.</div></div>","PeriodicalId":101065,"journal":{"name":"Redox Biochemistry and Chemistry","volume":"14 ","pages":"Article 100060"},"PeriodicalIF":0.0,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145107888","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

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Mapping oxylipin signatures in human diseases using LC-MS/MS 用LC-MS/MS绘制人类疾病中的氧脂质特征

Redox Biochemistry and Chemistry Pub Date : 2025-12-01 Epub Date: 2025-10-17 DOI: 10.1016/j.rbc.2025.100063

Larissa R. Diniz , Rosangela S. Santos , Hector Oreliana , Ana Clara A. Zucão, Megumi N. Yukuyama, Guilherme R.S. Resende, Thais Satie Iijima, Lucas G. Viviani, Sayuri Miyamoto

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State of the art in vivo reactive oxygen species measurements in skeletal muscle using fluorescent proteins 使用荧光蛋白测量骨骼肌体内活性氧的技术现状

Redox Biochemistry and Chemistry Pub Date : 2025-09-01 Epub Date: 2025-06-19 DOI: 10.1016/j.rbc.2025.100056

Ryotaro Kano , Hideki Shirakawa , David C. Poole , Daisuke Hoshino , Yutaka Kano

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Peroxidation rate constants and mechanisms of isoprenoid-derived lipids and their roles in ferroptosis 类异戊二烯类脂质过氧化速率常数和机制及其在铁下垂中的作用

Redox Biochemistry and Chemistry Pub Date : 2025-09-01 Epub Date: 2025-08-19 DOI: 10.1016/j.rbc.2025.100058

Noelle Reimers, Libin Xu

{"title":"Peroxidation rate constants and mechanisms of isoprenoid-derived lipids and their roles in ferroptosis","authors":"Noelle Reimers, Libin Xu","doi":"10.1016/j.rbc.2025.100058","DOIUrl":"10.1016/j.rbc.2025.100058","url":null,"abstract":"<div><div>Ferroptosis is a type of regulated cell death that is dependent on iron and driven by lipid peroxidation. Polyunsaturated fatty acids (PUFAs) sensitize cells to ferroptosis as they are prone to lipid peroxidation while monounsaturated fatty acids confer resistance to ferroptosis when incorporated into the lipid membrane as they are much less reactive toward lipid peroxidation. Recently, in addition to fatty acid-derived lipids, isoprenoid-derived lipids have been found to regulate ferroptosis. Specifically, ferroptosis suppressor protein 1 (FSP1) was found to be anti-ferroptotic as it reduces the oxidized forms of coenzyme Q<sub>10</sub> and vitamin K to their reduced quinol forms, which are phenolic radical-trapping antioxidants. Vitamins D<sub>3</sub> and A have also been found to inhibit ferroptosis in cancer cells. Furthermore, it has been shown that metabolites along the cholesterol synthesis pathway, including squalene, cholesterol, desmosterol, and 7-dehydrocholesterol (7-DHC), can protect cells against ferroptosis in vitro. Despite large variations in the reactivities of these lipids toward lipid peroxidation, they generally exhibit anti-ferroptotic properties. In this review, we will discuss the peroxidation rate constants and mechanisms of these isoprenoid-derived lipids and how they might contribute to their roles in ferroptosis.</div></div>","PeriodicalId":101065,"journal":{"name":"Redox Biochemistry and Chemistry","volume":"13 ","pages":"Article 100058"},"PeriodicalIF":0.0,"publicationDate":"2025-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144890329","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

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The chemistry of arachidonic acid oxygenation by prostaglandin endoperoxide synthase 前列腺素内过氧化物合酶催化花生四烯酸氧化的化学性质

Redox Biochemistry and Chemistry Pub Date : 2025-09-01 Epub Date: 2025-06-29 DOI: 10.1016/j.rbc.2025.100057

Lawrence J. Marnett

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Iodide influences the sensitized one-electron photo-oxidation of Tyr and Trp residues by competition reaction 碘化物通过竞争反应影响Tyr和Trp残基的敏化单电子光氧化

Redox Biochemistry and Chemistry Pub Date : 2025-06-01 Epub Date: 2025-04-13 DOI: 10.1016/j.rbc.2025.100050

M. Ignasiak , K.J. Frąckowiak , E. Fuentes-Lemus , P.M. Hägglund , L. Gamon , M.J. Davies , Ł. Marczak , B. Marciniak

{"title":"Iodide influences the sensitized one-electron photo-oxidation of Tyr and Trp residues by competition reaction","authors":"M. Ignasiak , K.J. Frąckowiak , E. Fuentes-Lemus , P.M. Hägglund , L. Gamon , M.J. Davies , Ł. Marczak , B. Marciniak","doi":"10.1016/j.rbc.2025.100050","DOIUrl":"10.1016/j.rbc.2025.100050","url":null,"abstract":"<div><div>3-carboxybenzophenone (CB) is an efficient photosensitizer that can oxidize multiple amino acid side chains in peptides and proteins <em>via</em> electron transfer (ET) reactions yielding various radicals and radical ions. Recombination reactions of these species can yield CBH-adducts and cross-links, whereas secondary reactions can give radicals on other side chains and further products. Prevention of initial radical formation, or interception of intermediate radicals is predicted to modulate the extent of protein damage. Consequently, in this work the effect of iodide ions (I‾) on CB-photosensitized oxidation was investigated with Trp and TyrOH, as these moieties are prone to photooxidation. A scavenging effect of I‾ on the formation of TyrO<sup>•</sup> radicals was readily detected in kinetic experiments using laser flash photolysis, whilst effects on TrpN<sup>•</sup> radical formation remain ambiguous (due to overlap of the absorptions of transient absorption spectra of TrpN<sup>•</sup> and CBH<sup>•</sup> radicals). Addition of I‾ suppresses oxidation of Trp and TyrOH, with this resulting in lower concentrations of di-Trp, di-Tyr and adducts with CBH, without formation of additional products involving I‾. The effect of I‾ was also analysed for a model protein – lysozyme – with a protective effect observed against loss of activity on illumination with CB. Multiple products were identified, including adducts of CBH to Trp, TyrOH or Met. The formation of crosslinks arising from CB-mediated photo-oxidation of lysozyme was limited in the presence of I‾. Together these data indicate that I‾ modulates photodamage induced by CB to peptide and protein targets.</div></div>","PeriodicalId":101065,"journal":{"name":"Redox Biochemistry and Chemistry","volume":"12 ","pages":"Article 100050"},"PeriodicalIF":0.0,"publicationDate":"2025-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143860747","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Chemical mechanisms of lipid peroxidation 脂质过氧化的化学机制

Redox Biochemistry and Chemistry Pub Date : 2025-06-01 Epub Date: 2025-05-26 DOI: 10.1016/j.rbc.2025.100054

Ned A. Porter

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Methionine oxidation products as biomarkers of oxidative damage to proteins and modulators of cellular metabolism and toxicity 蛋氨酸氧化产物作为蛋白质氧化损伤的生物标志物和细胞代谢和毒性调节剂

Redox Biochemistry and Chemistry Pub Date : 2025-06-01 Epub Date: 2025-05-05 DOI: 10.1016/j.rbc.2025.100052

Michael J. Davies

{"title":"Methionine oxidation products as biomarkers of oxidative damage to proteins and modulators of cellular metabolism and toxicity","authors":"Michael J. Davies","doi":"10.1016/j.rbc.2025.100052","DOIUrl":"10.1016/j.rbc.2025.100052","url":null,"abstract":"<div><div>Proteins are highly abundant and readily oxidized targets of reactive species formed in biological systems, with these often accounting for greater than 50 % of the dry mass of biological samples. Of the amino acids present in proteins, the sulfur-containing amino acids cysteine (Cys), cystine and methionine (Met) are some of the most reactive species with a range of biologically-relevant modifying agents including radicals, two-electron species and also many electrophiles. Reaction with Cys gives a wide range of both reversible and irreversible species. Lesser numbers of products are well-characterized for cystine and Met. For the latter, the sulfoxide is often the most abundant product, but other species including the cyclic species dehydromethionine, and methionine sulfone have been characterized and shown to be major species under some circumstances. Whilst the sulfone has been widely reported to arise from the sulfoxide as a result of further oxidation, increasing evidence suggests that it can also be formed directly, without the intermediacy of the sulfoxide, and particularly with singlet oxygen (<sup>1</sup>O<sub>2</sub>). Whilst the sulfoxide is subject to reduction (e.g. via methionine sulfoxide reductases) and further metabolism <em>in vivo</em>, the sulfone appears to be a stable product and may therefore under certain circumstances be a biomarker of Met oxidation. This article briefly reviews the oxidation chemistry of Cys and cystine, and a more detailed discussion of the mechanisms of Met oxidation, formation of the sulfoxide, dehydromethionine and sulfone, and the biological fates and activities of these species.</div></div>","PeriodicalId":101065,"journal":{"name":"Redox Biochemistry and Chemistry","volume":"12 ","pages":"Article 100052"},"PeriodicalIF":0.0,"publicationDate":"2025-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143912905","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

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