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Nitric oxide and hydrogen sulfide modulate the NADPH-generating enzymatic system in higher plants.
J Exp Bot. 2021 02 11; 72(3):830-847.JE

Abstract

Nitric oxide (NO) and hydrogen sulfide (H2S) are two key molecules in plant cells that participate, directly or indirectly, as regulators of protein functions through derived post-translational modifications, mainly tyrosine nitration, S-nitrosation, and persulfidation. These post-translational modifications allow the participation of both NO and H2S signal molecules in a wide range of cellular processes either physiological or under stressful circumstances. NADPH participates in cellular redox status and it is a key cofactor necessary for cell growth and development. It is involved in significant biochemical routes such as fatty acid, carotenoid and proline biosynthesis, and the shikimate pathway, as well as in cellular detoxification processes including the ascorbate-glutathione cycle, the NADPH-dependent thioredoxin reductase (NTR), or the superoxide-generating NADPH oxidase. Plant cells have diverse mechanisms to generate NADPH by a group of NADP-dependent oxidoreductases including ferredoxin-NADP reductase (FNR), NADP-glyceraldehyde-3-phosphate dehydrogenase (NADP-GAPDH), NADP-dependent malic enzyme (NADP-ME), NADP-dependent isocitrate dehydrogenase (NADP-ICDH), and both enzymes of the oxidative pentose phosphate pathway, designated as glucose-6-phosphate dehydrogenase (G6PDH) and 6-phosphogluconate dehydrogenase (6PGDH). These enzymes consist of different isozymes located in diverse subcellular compartments (chloroplasts, cytosol, mitochondria, and peroxisomes) which contribute to the NAPDH cellular pool. We provide a comprehensive overview of how post-translational modifications promoted by NO (tyrosine nitration and S-nitrosation), H2S (persulfidation), and glutathione (glutathionylation), affect the cellular redox status through regulation of the NADP-dependent dehydrogenases.

Authors+Show Affiliations

Group of Antioxidant, Free Radical and Nitric Oxide in Biotechnology, Food and Agriculture, Department of Biochemistry, Cell and Molecular Biology of Plants, Estación Experimental del Zaidín, CSIC, C/ Profesor Albareda, Granada, Spain.Group of Antioxidant, Free Radical and Nitric Oxide in Biotechnology, Food and Agriculture, Department of Biochemistry, Cell and Molecular Biology of Plants, Estación Experimental del Zaidín, CSIC, C/ Profesor Albareda, Granada, Spain.Group of Antioxidant, Free Radical and Nitric Oxide in Biotechnology, Food and Agriculture, Department of Biochemistry, Cell and Molecular Biology of Plants, Estación Experimental del Zaidín, CSIC, C/ Profesor Albareda, Granada, Spain.

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't
Review

Language

eng

PubMed ID

32945878

Citation

Corpas, Francisco J., et al. "Nitric Oxide and Hydrogen Sulfide Modulate the NADPH-generating Enzymatic System in Higher Plants." Journal of Experimental Botany, vol. 72, no. 3, 2021, pp. 830-847.
Corpas FJ, González-Gordo S, Palma JM. Nitric oxide and hydrogen sulfide modulate the NADPH-generating enzymatic system in higher plants. J Exp Bot. 2021;72(3):830-847.
Corpas, F. J., González-Gordo, S., & Palma, J. M. (2021). Nitric oxide and hydrogen sulfide modulate the NADPH-generating enzymatic system in higher plants. Journal of Experimental Botany, 72(3), 830-847. https://doi.org/10.1093/jxb/eraa440
Corpas FJ, González-Gordo S, Palma JM. Nitric Oxide and Hydrogen Sulfide Modulate the NADPH-generating Enzymatic System in Higher Plants. J Exp Bot. 2021 02 11;72(3):830-847. PubMed PMID: 32945878.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Nitric oxide and hydrogen sulfide modulate the NADPH-generating enzymatic system in higher plants. AU - Corpas,Francisco J, AU - González-Gordo,Salvador, AU - Palma,José M, PY - 2020/06/01/received PY - 2020/09/16/accepted PY - 2020/9/19/pubmed PY - 2021/5/21/medline PY - 2020/9/18/entrez KW - S-nitrosation KW - 6-phosphogluconate dehydrogenase KW - Glucose-6-phosphate dehydrogenase KW - NADP-isocitrate dehydrogenase KW - NADPH KW - glutathionylation KW - hydrogen sulfide KW - nitric oxide KW - persulfidation KW - tyrosine nitration SP - 830 EP - 847 JF - Journal of experimental botany JO - J Exp Bot VL - 72 IS - 3 N2 - Nitric oxide (NO) and hydrogen sulfide (H2S) are two key molecules in plant cells that participate, directly or indirectly, as regulators of protein functions through derived post-translational modifications, mainly tyrosine nitration, S-nitrosation, and persulfidation. These post-translational modifications allow the participation of both NO and H2S signal molecules in a wide range of cellular processes either physiological or under stressful circumstances. NADPH participates in cellular redox status and it is a key cofactor necessary for cell growth and development. It is involved in significant biochemical routes such as fatty acid, carotenoid and proline biosynthesis, and the shikimate pathway, as well as in cellular detoxification processes including the ascorbate-glutathione cycle, the NADPH-dependent thioredoxin reductase (NTR), or the superoxide-generating NADPH oxidase. Plant cells have diverse mechanisms to generate NADPH by a group of NADP-dependent oxidoreductases including ferredoxin-NADP reductase (FNR), NADP-glyceraldehyde-3-phosphate dehydrogenase (NADP-GAPDH), NADP-dependent malic enzyme (NADP-ME), NADP-dependent isocitrate dehydrogenase (NADP-ICDH), and both enzymes of the oxidative pentose phosphate pathway, designated as glucose-6-phosphate dehydrogenase (G6PDH) and 6-phosphogluconate dehydrogenase (6PGDH). These enzymes consist of different isozymes located in diverse subcellular compartments (chloroplasts, cytosol, mitochondria, and peroxisomes) which contribute to the NAPDH cellular pool. We provide a comprehensive overview of how post-translational modifications promoted by NO (tyrosine nitration and S-nitrosation), H2S (persulfidation), and glutathione (glutathionylation), affect the cellular redox status through regulation of the NADP-dependent dehydrogenases. SN - 1460-2431 UR - https://www.unboundmedicine.com/medline/citation/32945878/Nitric_oxide_and_hydrogen_sulfide_modulate_the_NADPH_generating_enzymatic_system_in_higher_plants_ L2 - https://academic.oup.com/jxb/article-lookup/doi/10.1093/jxb/eraa440 DB - PRIME DP - Unbound Medicine ER -