Soybean (Glycine max L.) Lipoxygenase 1 (LOX 1) is modulated by nitric oxide and hydrogen sulfide: an in vitro approach

Hydrogen sulfide (H2S) and nitric oxide (NO) are two relevant signal molecules that can affect protein function throughout post-translational modifications (PTMs) such as persulfidation, S-nitrosation, metal-nitrosylation, and nitration. Lipoxygenases (LOXs) are a group of non-heme iron enzymes invo...

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Autores: González-Gordo, Salvador, López-Jaramillo, Javier, Palma Martínez, José Manuel, Corpas, Francisco J.
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2023
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/308148
Acceso en línea:http://hdl.handle.net/10261/308148
Access Level:acceso abierto
Palabra clave:Hydrogen sulfide
Lipoxygenase
Nitric oxide
Peroxynitrite
Post-translational modification
Protein modeling
Tyrosine nitration
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spelling Soybean (Glycine max L.) Lipoxygenase 1 (LOX 1) is modulated by nitric oxide and hydrogen sulfide: an in vitro approachGonzález-Gordo, SalvadorLópez-Jaramillo, JavierPalma Martínez, José ManuelCorpas, Francisco J.Hydrogen sulfideLipoxygenaseNitric oxidePeroxynitritePost-translational modificationProtein modelingTyrosine nitrationHydrogen sulfide (H2S) and nitric oxide (NO) are two relevant signal molecules that can affect protein function throughout post-translational modifications (PTMs) such as persulfidation, S-nitrosation, metal-nitrosylation, and nitration. Lipoxygenases (LOXs) are a group of non-heme iron enzymes involved in a wide range of plant physiological functions including seed germination, plant growth and development, and fruit ripening and senescence. Likewise, LOXs are also involved in the mechanisms of response to diverse environmental stresses. Using purified soybean (Glycine max L.) lipoxygenase type 1 (LOX 1) and nitrosocysteine (CysNO) and sodium hydrosulfide (NaHS) as NO and H2S donors, respectively, the present study reveals that both compounds negatively affect LOX activity, suggesting that S-nitrosation and persulfidation are involved. Mass spectrometric analysis of nitrated soybean LOX 1 using a peroxynitrite (ONOO−) donor enabled us to identify that, among the thirty-five tyrosine residues present in this enzyme, only Y214 was exclusively nitrated by ONOO−. The nitration of Y214 seems to affect its interaction with W500, a residue involved in the substrate binding site. The analysis of the structure 3PZW demonstrates the existence of several tunnels that directly communicate the surface of the protein with different internal cysteines, thus making feasible their potential persulfidation, especially C429 and C127. On the other hand, the CysNO molecule, which is hydrophilic and bulkier than H2S, can somehow be accommodated throughout the tunnel until it reaches C127, thus facilitating its nitrosation. Overall, a large number of potential persulfidation targets and the ease by which H2S can reach them through the diffuse tunneling network could be behind their efficient inhibition.Our research is supported by European Regional Development Fund co-financed grants from the Ministry of Science and Innovation (PID2019-103924GB-I00), the AEI (10.13039/501100011033), and Junta de Andalucía (P18-FR-1359), Spain.Peer reviewedMultidisciplinary Digital Publishing InstituteEuropean CommissionMinisterio de Ciencia, Innovación y Universidades (España)Agencia Estatal de Investigación (España)Junta de AndalucíaConsejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]2023202320232023info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Publisher's versioninfo:eu-repo/semantics/publishedVersionapplication/pdfhttp://hdl.handle.net/10261/308148reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Inglés#PLACEHOLDER_PARENT_METADATA_VALUE#info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2017-2020/PID2019-103924GB-I00https://doi.org/10.3390/ijms24098001Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/3081482026-05-22T06:33:51Z
dc.title.none.fl_str_mv Soybean (Glycine max L.) Lipoxygenase 1 (LOX 1) is modulated by nitric oxide and hydrogen sulfide: an in vitro approach
title Soybean (Glycine max L.) Lipoxygenase 1 (LOX 1) is modulated by nitric oxide and hydrogen sulfide: an in vitro approach
spellingShingle Soybean (Glycine max L.) Lipoxygenase 1 (LOX 1) is modulated by nitric oxide and hydrogen sulfide: an in vitro approach
González-Gordo, Salvador
Hydrogen sulfide
Lipoxygenase
Nitric oxide
Peroxynitrite
Post-translational modification
Protein modeling
Tyrosine nitration
title_short Soybean (Glycine max L.) Lipoxygenase 1 (LOX 1) is modulated by nitric oxide and hydrogen sulfide: an in vitro approach
title_full Soybean (Glycine max L.) Lipoxygenase 1 (LOX 1) is modulated by nitric oxide and hydrogen sulfide: an in vitro approach
title_fullStr Soybean (Glycine max L.) Lipoxygenase 1 (LOX 1) is modulated by nitric oxide and hydrogen sulfide: an in vitro approach
title_full_unstemmed Soybean (Glycine max L.) Lipoxygenase 1 (LOX 1) is modulated by nitric oxide and hydrogen sulfide: an in vitro approach
title_sort Soybean (Glycine max L.) Lipoxygenase 1 (LOX 1) is modulated by nitric oxide and hydrogen sulfide: an in vitro approach
dc.creator.none.fl_str_mv González-Gordo, Salvador
López-Jaramillo, Javier
Palma Martínez, José Manuel
Corpas, Francisco J.
author González-Gordo, Salvador
author_facet González-Gordo, Salvador
López-Jaramillo, Javier
Palma Martínez, José Manuel
Corpas, Francisco J.
author_role author
author2 López-Jaramillo, Javier
Palma Martínez, José Manuel
Corpas, Francisco J.
author2_role author
author
author
dc.contributor.none.fl_str_mv European Commission
Ministerio de Ciencia, Innovación y Universidades (España)
Agencia Estatal de Investigación (España)
Junta de Andalucía
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv Hydrogen sulfide
Lipoxygenase
Nitric oxide
Peroxynitrite
Post-translational modification
Protein modeling
Tyrosine nitration
topic Hydrogen sulfide
Lipoxygenase
Nitric oxide
Peroxynitrite
Post-translational modification
Protein modeling
Tyrosine nitration
description Hydrogen sulfide (H2S) and nitric oxide (NO) are two relevant signal molecules that can affect protein function throughout post-translational modifications (PTMs) such as persulfidation, S-nitrosation, metal-nitrosylation, and nitration. Lipoxygenases (LOXs) are a group of non-heme iron enzymes involved in a wide range of plant physiological functions including seed germination, plant growth and development, and fruit ripening and senescence. Likewise, LOXs are also involved in the mechanisms of response to diverse environmental stresses. Using purified soybean (Glycine max L.) lipoxygenase type 1 (LOX 1) and nitrosocysteine (CysNO) and sodium hydrosulfide (NaHS) as NO and H2S donors, respectively, the present study reveals that both compounds negatively affect LOX activity, suggesting that S-nitrosation and persulfidation are involved. Mass spectrometric analysis of nitrated soybean LOX 1 using a peroxynitrite (ONOO−) donor enabled us to identify that, among the thirty-five tyrosine residues present in this enzyme, only Y214 was exclusively nitrated by ONOO−. The nitration of Y214 seems to affect its interaction with W500, a residue involved in the substrate binding site. The analysis of the structure 3PZW demonstrates the existence of several tunnels that directly communicate the surface of the protein with different internal cysteines, thus making feasible their potential persulfidation, especially C429 and C127. On the other hand, the CysNO molecule, which is hydrophilic and bulkier than H2S, can somehow be accommodated throughout the tunnel until it reaches C127, thus facilitating its nitrosation. Overall, a large number of potential persulfidation targets and the ease by which H2S can reach them through the diffuse tunneling network could be behind their efficient inhibition.
publishDate 2023
dc.date.none.fl_str_mv 2023
2023
2023
2023
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
Publisher's version
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/308148
url http://hdl.handle.net/10261/308148
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv #PLACEHOLDER_PARENT_METADATA_VALUE#
info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2017-2020/PID2019-103924GB-I00
https://doi.org/10.3390/ijms24098001
Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Multidisciplinary Digital Publishing Institute
publisher.none.fl_str_mv Multidisciplinary Digital Publishing Institute
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
repository.name.fl_str_mv
repository.mail.fl_str_mv
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