Francisco J. Corpas , Jorge Taboada , Beatriz Sánchez-Romera , Javier López-Jaramillo , José M. Palma
{"title":"硫酸盐过氧化物酶体氧化酶(SOX)是高等植物一氧化氮的替代来源,可被H2S上调","authors":"Francisco J. Corpas , Jorge Taboada , Beatriz Sánchez-Romera , Javier López-Jaramillo , José M. Palma","doi":"10.1016/j.plaphy.2025.110000","DOIUrl":null,"url":null,"abstract":"<div><div>Nitric oxide (<sup>•</sup>NO) is a free radical that is endogenously produced in plant cells, though its enzymatic synthesis remains a subject of ongoing debate. Plant peroxisomes, subcellular compartments with active nitro-oxidative metabolism, play a role in various metabolic pathways. Sulfite oxidase (SOX), a peroxisomal enzyme requiring the molybdenum cofactor (MoCo), catalyzes the oxidation of sulfite (SO<sub>3</sub><sup>2−</sup>) to sulfate (SO<sub>4</sub><sup>2−</sup>), along with the concomitant production of H<sub>2</sub>O<sub>2</sub>. Using reconstituted recombinant SOX from pepper (<em>Capsicum annuum</em> L.) fruit, it was shown that this enzyme has the capacity to generate <sup>•</sup>NO using nitrite (NO<sub>2</sub><sup>−</sup>) as a substrate and NADH as an electron donor which was detected by electron paramagnetic resonance (EPR) spectroscopy coupled with the spin-trapping method. Furthermore, this <sup>•</sup>NO generation was upregulated in the presence of hydrogen sulfide (H<sub>2</sub>S) but was downregulated by H<sub>2</sub>O<sub>2</sub> which highlights the relationship between H<sub>2</sub>O<sub>2</sub>, <sup>•</sup>NO, and H<sub>2</sub>S. This data opens new avenues for understanding the enzymatic sources of <sup>•</sup>NO in higher plants, particularly within peroxisomes.</div></div>","PeriodicalId":20234,"journal":{"name":"Plant Physiology and Biochemistry","volume":"225 ","pages":"Article 110000"},"PeriodicalIF":6.1000,"publicationDate":"2025-05-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Peroxisomal Sulfite Oxidase (SOX), an alternative source of NO in higher plants which is upregulated by H2S\",\"authors\":\"Francisco J. Corpas , Jorge Taboada , Beatriz Sánchez-Romera , Javier López-Jaramillo , José M. Palma\",\"doi\":\"10.1016/j.plaphy.2025.110000\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><div>Nitric oxide (<sup>•</sup>NO) is a free radical that is endogenously produced in plant cells, though its enzymatic synthesis remains a subject of ongoing debate. Plant peroxisomes, subcellular compartments with active nitro-oxidative metabolism, play a role in various metabolic pathways. Sulfite oxidase (SOX), a peroxisomal enzyme requiring the molybdenum cofactor (MoCo), catalyzes the oxidation of sulfite (SO<sub>3</sub><sup>2−</sup>) to sulfate (SO<sub>4</sub><sup>2−</sup>), along with the concomitant production of H<sub>2</sub>O<sub>2</sub>. Using reconstituted recombinant SOX from pepper (<em>Capsicum annuum</em> L.) fruit, it was shown that this enzyme has the capacity to generate <sup>•</sup>NO using nitrite (NO<sub>2</sub><sup>−</sup>) as a substrate and NADH as an electron donor which was detected by electron paramagnetic resonance (EPR) spectroscopy coupled with the spin-trapping method. Furthermore, this <sup>•</sup>NO generation was upregulated in the presence of hydrogen sulfide (H<sub>2</sub>S) but was downregulated by H<sub>2</sub>O<sub>2</sub> which highlights the relationship between H<sub>2</sub>O<sub>2</sub>, <sup>•</sup>NO, and H<sub>2</sub>S. This data opens new avenues for understanding the enzymatic sources of <sup>•</sup>NO in higher plants, particularly within peroxisomes.</div></div>\",\"PeriodicalId\":20234,\"journal\":{\"name\":\"Plant Physiology and Biochemistry\",\"volume\":\"225 \",\"pages\":\"Article 110000\"},\"PeriodicalIF\":6.1000,\"publicationDate\":\"2025-05-09\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Plant Physiology and Biochemistry\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S0981942825005285\",\"RegionNum\":2,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"PLANT SCIENCES\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Plant Physiology and Biochemistry","FirstCategoryId":"99","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0981942825005285","RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"PLANT SCIENCES","Score":null,"Total":0}
Peroxisomal Sulfite Oxidase (SOX), an alternative source of NO in higher plants which is upregulated by H2S
Nitric oxide (•NO) is a free radical that is endogenously produced in plant cells, though its enzymatic synthesis remains a subject of ongoing debate. Plant peroxisomes, subcellular compartments with active nitro-oxidative metabolism, play a role in various metabolic pathways. Sulfite oxidase (SOX), a peroxisomal enzyme requiring the molybdenum cofactor (MoCo), catalyzes the oxidation of sulfite (SO32−) to sulfate (SO42−), along with the concomitant production of H2O2. Using reconstituted recombinant SOX from pepper (Capsicum annuum L.) fruit, it was shown that this enzyme has the capacity to generate •NO using nitrite (NO2−) as a substrate and NADH as an electron donor which was detected by electron paramagnetic resonance (EPR) spectroscopy coupled with the spin-trapping method. Furthermore, this •NO generation was upregulated in the presence of hydrogen sulfide (H2S) but was downregulated by H2O2 which highlights the relationship between H2O2, •NO, and H2S. This data opens new avenues for understanding the enzymatic sources of •NO in higher plants, particularly within peroxisomes.
期刊介绍:
Plant Physiology and Biochemistry publishes original theoretical, experimental and technical contributions in the various fields of plant physiology (biochemistry, physiology, structure, genetics, plant-microbe interactions, etc.) at diverse levels of integration (molecular, subcellular, cellular, organ, whole plant, environmental). Opinions expressed in the journal are the sole responsibility of the authors and publication does not imply the editors'' agreement.
Manuscripts describing molecular-genetic and/or gene expression data that are not integrated with biochemical analysis and/or actual measurements of plant physiological processes are not suitable for PPB. Also "Omics" studies (transcriptomics, proteomics, metabolomics, etc.) reporting descriptive analysis without an element of functional validation assays, will not be considered. Similarly, applied agronomic or phytochemical studies that generate no new, fundamental insights in plant physiological and/or biochemical processes are not suitable for publication in PPB.
Plant Physiology and Biochemistry publishes several types of articles: Reviews, Papers and Short Papers. Articles for Reviews are either invited by the editor or proposed by the authors for the editor''s prior agreement. Reviews should not exceed 40 typewritten pages and Short Papers no more than approximately 8 typewritten pages. The fundamental character of Plant Physiology and Biochemistry remains that of a journal for original results.