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dc.contributor.author | Sainz, Martha | es_ES |
dc.contributor.author | Pérez-Rontomé, Carmen | es_ES |
dc.contributor.author | Ramos, Javier | es_ES |
dc.contributor.author | Mulet Salort, José Miguel | es_ES |
dc.contributor.author | James, Euan K. | es_ES |
dc.contributor.author | Bhattacharjee, Ujjal | es_ES |
dc.contributor.author | Petrich, Jacob W. | es_ES |
dc.contributor.author | Becana, Manuel | es_ES |
dc.date.accessioned | 2016-01-14T10:02:57Z | |
dc.date.available | 2016-01-14T10:02:57Z | |
dc.date.issued | 2013-12 | |
dc.identifier.issn | 0960-7412 | |
dc.identifier.uri | http://hdl.handle.net/10251/59876 | |
dc.description | This is the accepted version of the following article: Sainz, M., Pérez-Rontomé, C., Ramos, J., Mulet, J. M., James, E. K., Bhattacharjee, U., Petrich, J. W. and Becana, M. (2013), Plant hemoglobins may be maintained in functional form by reduced flavins in the nuclei, and confer differential tolerance to nitro-oxidative stress. Plant J, 76: 875–887, which has been published in final form at http://dx.doi.org/10.1111/tpj.12340. | es_ES |
dc.description.abstract | The heme of bacteria, plant and animal hemoglobins (Hbs) must be in the ferrous state to bind O2 and other physiological ligands. Here we have characterized the full set of non-symbiotic (class 1 and 2) and truncated (class 3) Hbs of Lotus japonicus. Class 1 Hbs are hexacoordinate, but class 2 and 3 Hbs are pentacoordinate. Three of the globins, Glb1-1, Glb2 and Glb3-1, are nodule-enhanced proteins. The O2 affinity of Glb1-1 (50 pM) was the highest known for any Hb, and the protein may function as an O2 scavenger. The five globins were reduced by free flavins, which transfer electrons from NAD(P)H to the heme iron under aerobic and anaerobic conditions. Class 1 Hbs were reduced at very fast rates by FAD, class 2 Hbs at slower rates by both FMN and FAD, and class 3 Hbs at intermediate rates by FMN. The members of the three globin classes were immunolocalized predominantly in the nuclei. Flavins were quantified in legume nodules and nuclei, and their concentrations were sufficient to maintain Hbs in their functional state. All Hbs, except Glb1-1, were expressed in a flavohemoglobin-deficient yeast mutant and found to confer tolerance to oxidative stress induced by methyl viologen, copper or low temperature, indicating an anti-oxidative role for the hemes. However, only Glb1-2 and Glb2 afforded protection against nitrosative stress induced by S-nitrosoglutathione. Because this compound is specifically involved in transnitrosylation reactions with thiol groups, our results suggest a contribution of the single cysteine residues of both proteins in the stress response. | es_ES |
dc.description.sponsorship | We are grateful to Ryan Sturms and Mark Hargrove (Department of Biochemistry and Molecular Biology, Iowa State University, Ames, IA) for help with stopped-flow measurements, and to Raul Arredondo-Peter (Laboratorio de Biofisica y Biologia Molecular, Universidad Autonoma del Estado de Morelos, Mexico) and two anonymous reviewers for helpful comments on the manuscript. Thanks are also due to Laura Calvo, Ana Castillo and Ana Alvarez for help with protein purification, nuclei isolation and HPLC-MS analysis, respectively. This work was funded by the Spanish Ministry of Economy and Competitiveness/Fondo Europeo de Desarrollo Regional (grant AGL2011-24524) and the Government of Aragon/Fondo Social Europeo (group A53). M. S. was supported by a pre-doctoral contract from Junta de Ampliacion de Estudios/Consejo Superior de Investigaciones Cientificas. | en_EN |
dc.language | Inglés | es_ES |
dc.publisher | Wiley-Blackwell | es_ES |
dc.relation.ispartof | The Plant Journal | es_ES |
dc.rights | Reserva de todos los derechos | es_ES |
dc.subject | Lotus japonicus | es_ES |
dc.subject | Plant hemoglobins | es_ES |
dc.subject | Flavins | es_ES |
dc.subject | Legume nodules | es_ES |
dc.subject | Nitrosative stress | es_ES |
dc.subject | Oxidative stress | es_ES |
dc.subject.classification | BIOQUIMICA Y BIOLOGIA MOLECULAR | es_ES |
dc.title | Plant hemoglobins may be maintained in functional form by reduced flavins in the nuclei, and confer differential tolerance to nitro-oxidative stress | es_ES |
dc.type | Artículo | es_ES |
dc.identifier.doi | 10.1111/tpj.12340 | |
dc.relation.projectID | info:eu-repo/grantAgreement/MICINN//AGL2011-24524/ES/SEÑALIZACION POR ESPECIES REACTIVAS DE OXIGENO%2FNITROGENO Y ANTIOXIDANTES EN LA SIMBIOSIS FIJADORA DE NITROGENO RHIZOBIUM-LEGUMINOSA/ | es_ES |
dc.rights.accessRights | Abierto | es_ES |
dc.contributor.affiliation | Universitat Politècnica de València. Departamento de Biotecnología - Departament de Biotecnologia | es_ES |
dc.contributor.affiliation | Universitat Politècnica de València. Instituto Universitario Mixto de Biología Molecular y Celular de Plantas - Institut Universitari Mixt de Biologia Molecular i Cel·lular de Plantes | es_ES |
dc.description.bibliographicCitation | Sainz, M.; Pérez-Rontomé, C.; Ramos, J.; Mulet Salort, JM.; James, EK.; Bhattacharjee, U.; Petrich, JW.... (2013). Plant hemoglobins may be maintained in functional form by reduced flavins in the nuclei, and confer differential tolerance to nitro-oxidative stress. The Plant Journal. 76(5):875-887. https://doi.org/10.1111/tpj.12340 | es_ES |
dc.description.accrualMethod | S | es_ES |
dc.relation.publisherversion | http://dx.doi.org/10.1111/tpj.12340 | es_ES |
dc.description.upvformatpinicio | 875 | es_ES |
dc.description.upvformatpfin | 887 | es_ES |
dc.type.version | info:eu-repo/semantics/publishedVersion | es_ES |
dc.description.volume | 76 | es_ES |
dc.description.issue | 5 | es_ES |
dc.relation.senia | 252959 | es_ES |
dc.identifier.eissn | 1365-313X | |
dc.contributor.funder | Ministerio de Ciencia e Innovación | es_ES |
dc.contributor.funder | European Social Fund | es_ES |
dc.contributor.funder | Gobierno de Aragón | es_ES |
dc.description.references | Angelo, M., Hausladen, A., Singel, D. J., & Stamler, J. S. (2008). Interactions of NO with Hemoglobin: From Microbes to Man. Globins and Other Nitric Oxide-Reactive Proteins, Part A, 131-168. doi:10.1016/s0076-6879(08)36008-x | es_ES |
dc.description.references | Appleby, C. A. (1984). Leghemoglobin and Rhizobium Respiration. Annual Review of Plant Physiology, 35(1), 443-478. doi:10.1146/annurev.pp.35.060184.002303 | es_ES |
dc.description.references | Baudouin, E. (2003). A Medicago sativa haem oxygenase gene is preferentially expressed in root nodules. Journal of Experimental Botany, 55(394), 43-47. doi:10.1093/jxb/erh020 | es_ES |
dc.description.references | Becana, M., & Klucas, R. V. (1990). Enzymatic and nonenzymatic mechanisms for ferric leghemoglobin reduction in legume root nodules. Proceedings of the National Academy of Sciences, 87(18), 7295-7299. doi:10.1073/pnas.87.18.7295 | es_ES |
dc.description.references | Becana, M., Matamoros, M. A., Udvardi, M., & Dalton, D. A. (2010). Recent insights into antioxidant defenses of legume root nodules. New Phytologist, 188(4), 960-976. doi:10.1111/j.1469-8137.2010.03512.x | es_ES |
dc.description.references | Bruno, S., Faggiano, S., Spyrakis, F., Mozzarelli, A., Abbruzzetti, S., Grandi, E., … Dominici, P. (2007). The Reactivity with CO of AHb1 and AHb2 fromArabidopsisthalianais Controlled by the Distal HisE7 and Internal Hydrophobic Cavities. Journal of the American Chemical Society, 129(10), 2880-2889. doi:10.1021/ja066638d | es_ES |
dc.description.references | Bustos-Sanmamed, P., Tovar-Méndez, A., Crespi, M., Sato, S., Tabata, S., & Becana, M. (2010). Regulation of nonsymbiotic and truncated hemoglobin genes of Lotus japonicus in plant organs and in response to nitric oxide and hormones. New Phytologist, 189(3), 765-776. doi:10.1111/j.1469-8137.2010.03527.x | es_ES |
dc.description.references | Bykova, N. V., Igamberdiev, A. U., Ens, W., & Hill, R. D. (2006). Identification of an intermolecular disulfide bond in barley hemoglobin. Biochemical and Biophysical Research Communications, 347(1), 301-309. doi:10.1016/j.bbrc.2006.06.091 | es_ES |
dc.description.references | Cochemé, H. M., & Murphy, M. P. (2007). Complex I Is the Major Site of Mitochondrial Superoxide Production by Paraquat. Journal of Biological Chemistry, 283(4), 1786-1798. doi:10.1074/jbc.m708597200 | es_ES |
dc.description.references | Dalton, D. A., Baird, L. M., Langeberg, L., Taugher, C. Y., Anyan, W. R., Vance, C. P., & Sarath, G. (1993). Subcellular Localization of Oxygen Defense Enzymes in Soybean (Glycine max [L.] Merr.) Root Nodules. Plant Physiology, 102(2), 481-489. doi:10.1104/pp.102.2.481 | es_ES |
dc.description.references | DORDAS, C. (2003). Plant Haemoglobins, Nitric Oxide and Hypoxic Stress. Annals of Botany, 91(2), 173-178. doi:10.1093/aob/mcf115 | es_ES |
dc.description.references | Duff, S. M. G., Wittenberg, J. B., & Hill, R. D. (1997). Expression, Purification, and Properties of Recombinant Barley (Hordeumsp.) Hemoglobin. Journal of Biological Chemistry, 272(27), 16746-16752. doi:10.1074/jbc.272.27.16746 | es_ES |
dc.description.references | Folta, K. M., & Kaufman, L. S. (2000). Preparation of transcriptionally active nuclei from etiolated Arabidopsis thaliana. Plant Cell Reports, 19(5), 504-510. doi:10.1007/s002990050764 | es_ES |
dc.description.references | Gardner, P. R. (2012). Hemoglobin: A Nitric-Oxide Dioxygenase. Scientifica, 2012, 1-34. doi:10.6064/2012/683729 | es_ES |
dc.description.references | Daniel Gietz, R., & Woods, R. A. (2002). Transformation of yeast by lithium acetate/single-stranded carrier DNA/polyethylene glycol method. Methods in Enzymology, 87-96. doi:10.1016/s0076-6879(02)50957-5 | es_ES |
dc.description.references | Gladwin, M. T., Ognibene, F. P., Pannell, L. K., Nichols, J. S., Pease-Fye, M. E., Shelhamer, J. H., & Schechter, A. N. (2000). Relative role of heme nitrosylation and beta -cysteine 93 nitrosation in the transport and metabolism of nitric oxide by hemoglobin in the human circulation. Proceedings of the National Academy of Sciences, 97(18), 9943-9948. doi:10.1073/pnas.180155397 | es_ES |
dc.description.references | Gupta, K. J., Fernie, A. R., Kaiser, W. M., & van Dongen, J. T. (2011). On the origins of nitric oxide. Trends in Plant Science, 16(3), 160-168. doi:10.1016/j.tplants.2010.11.007 | es_ES |
dc.description.references | Hargrove, M. S. (2000). A Flash Photolysis Method to Characterize Hexacoordinate Hemoglobin Kinetics. Biophysical Journal, 79(5), 2733-2738. doi:10.1016/s0006-3495(00)76512-x | es_ES |
dc.description.references | Hebelstrup, K. H., & Jensen, E. Ø. (2007). Expression of NO scavenging hemoglobin is involved in the timing of bolting in Arabidopsis thaliana. Planta, 227(4), 917-927. doi:10.1007/s00425-007-0667-z | es_ES |
dc.description.references | Hebelstrup, K. H., Igamberdiev, A. U., & Hill, R. D. (2007). Metabolic effects of hemoglobin gene expression in plants. Gene, 398(1-2), 86-93. doi:10.1016/j.gene.2007.01.039 | es_ES |
dc.description.references | Hebelstrup, K. H., Shah, J. K., & Igamberdiev, A. U. (2013). The role of nitric oxide and hemoglobin in plant development and morphogenesis. Physiologia Plantarum, 148(4), 457-469. doi:10.1111/ppl.12062 | es_ES |
dc.description.references | Hill, R. D. (2012). Non-symbiotic haemoglobins—What’s happening beyond nitric oxide scavenging? AoB PLANTS, 2012. doi:10.1093/aobpla/pls004 | es_ES |
dc.description.references | Hunt, P. W., Watts, R. A., Trevaskis, B., Llewelyn, D. J., Burnell, J., Dennis, E. S., & Peacock, W. J. (2001). Plant Molecular Biology, 47(5), 677-692. doi:10.1023/a:1012440926982 | es_ES |
dc.description.references | Hunt, P. W., Klok, E. J., Trevaskis, B., Watts, R. A., Ellis, M. H., Peacock, W. J., & Dennis, E. S. (2002). Increased level of hemoglobin 1 enhances survival of hypoxic stress and promotes early growth in Arabidopsis thaliana. Proceedings of the National Academy of Sciences, 99(26), 17197-17202. doi:10.1073/pnas.212648799 | es_ES |
dc.description.references | Igamberdiev, A. U., Bykova, N. V., & Hill, R. D. (2005). Nitric oxide scavenging by barley hemoglobin is facilitated by a monodehydroascorbate reductase-mediated ascorbate reduction of methemoglobin. Planta, 223(5), 1033-1040. doi:10.1007/s00425-005-0146-3 | es_ES |
dc.description.references | Igamberdiev, A. U., Bykova, N. V., Shah, J. K., & Hill, R. D. (2010). Anoxic nitric oxide cycling in plants: participating reactions and possible mechanisms. Physiologia Plantarum, 138(4), 393-404. doi:10.1111/j.1399-3054.2009.01314.x | es_ES |
dc.description.references | Ioanitescu, A. I., Dewilde, S., Kiger, L., Marden, M. C., Moens, L., & Van Doorslaer, S. (2005). Characterization of Nonsymbiotic Tomato Hemoglobin. Biophysical Journal, 89(4), 2628-2639. doi:10.1529/biophysj.105.060582 | es_ES |
dc.description.references | Kakar, S., Hoffman, F. G., Storz, J. F., Fabian, M., & Hargrove, M. S. (2010). Structure and reactivity of hexacoordinate hemoglobins. Biophysical Chemistry, 152(1-3), 1-14. doi:10.1016/j.bpc.2010.08.008 | es_ES |
dc.description.references | Kim, D. Y., Hong, M. J., Lee, Y. J., Lee, M. B., & Seo, Y. W. (2012). Wheat truncated hemoglobin interacts with photosystem I PSK-I subunit and photosystem II subunit PsbS1. Biologia Plantarum, 57(2), 281-290. doi:10.1007/s10535-012-0268-y | es_ES |
dc.description.references | Lee, H., Kim, H., & An, C. S. (2004). Cloning and expression analysis of 2-on-2 hemoglobin from soybean. Journal of Plant Biology, 47(2), 92-98. doi:10.1007/bf03030637 | es_ES |
dc.description.references | Miyake, C., Schreiber, U., Hormann, H., Sano, S., & Kozi, A. (1998). The FAD-Enzyme Monodehydroascorbate Radical Reductase Mediates Photoproduction of Superoxide Radicals in Spinach Thylakoid Membranes. Plant and Cell Physiology, 39(8), 821-829. doi:10.1093/oxfordjournals.pcp.a029440 | es_ES |
dc.description.references | Moran, J. F., Sun, Z., Sarath, G., Arredondo-Peter, R., James, E. K., Becana, M., & Klucas, R. V. (2002). Molecular Cloning, Functional Characterization, and Subcellular Localization of Soybean Nodule Dihydrolipoamide Reductase. Plant Physiology, 128(1), 300-313. doi:10.1104/pp.010505 | es_ES |
dc.description.references | Mulet, J. M., Alemany, B., Ros, R., Calvete, J. J., & Serrano, R. (2004). Expression of a plant serine O-acetyltransferase inSaccharomyces cerevisiae confers osmotic tolerance and creates an alternative pathway for cysteine biosynthesis. Yeast, 21(4), 303-312. doi:10.1002/yea.1076 | es_ES |
dc.description.references | Mur, L. A. J., Mandon, J., Persijn, S., Cristescu, S. M., Moshkov, I. E., Novikova, G. V., … Gupta, K. J. (2012). Nitric oxide in plants: an assessment of the current state of knowledge. AoB Plants, 5(0), pls052-pls052. doi:10.1093/aobpla/pls052 | es_ES |
dc.description.references | Pankhurst, C. E., Schwinghamer, E. A., Thorne, S. W., & Bergersen, F. J. (1974). The Flavin Content of Clovers Relative to Symbiosis with a Riboflavin-requiring Mutant of Rhizobium trifoli. Plant Physiology, 53(2), 198-205. doi:10.1104/pp.53.2.198 | es_ES |
dc.description.references | Perazzolli, M., Dominici, P., Romero-Puertas, M. C., Zago, E., Zeier, J., Sonoda, M., … Delledonne, M. (2004). Arabidopsis Nonsymbiotic Hemoglobin AHb1 Modulates Nitric Oxide Bioactivity. The Plant Cell, 16(10), 2785-2794. doi:10.1105/tpc.104.025379 | es_ES |
dc.description.references | Qu, Z.-L., Wang, H.-Y., & Xia, G.-X. (2005). GhHb1: A nonsymbiotic hemoglobin gene of cotton responsive to infection by Verticillium dahliae. Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression, 1730(2), 103-113. doi:10.1016/j.bbaexp.2005.06.009 | es_ES |
dc.description.references | Ríos, G., Cabedo, M., Rull, B., Yenush, L., Serrano, R., & Mulet, J. M. (2013). Role of the yeast multidrug transporter Qdr2 in cation homeostasis and the oxidative stress response. FEMS Yeast Research, 13(1), 97-106. doi:10.1111/1567-1364.12013 | es_ES |
dc.description.references | Rodríguez-Celma, J., Vázquez-Reina, S., Orduna, J., Abadía, A., Abadía, J., Álvarez-Fernández, A., & López-Millán, A.-F. (2011). Characterization of Flavins in Roots of Fe-Deficient Strategy I Plants, with a Focus on Medicago truncatula. Plant and Cell Physiology, 52(12), 2173-2189. doi:10.1093/pcp/pcr149 | es_ES |
dc.description.references | Ross, E. J. H., Shearman, L., Mathiesen, M., Zhou, Y. J., Arredondo-Peter, R., Sarath, G., & Klucas, R. V. (2001). Nonsymbiotic hemoglobins in rice are synthesized during germination and in differentiating cell types. Protoplasma, 218(3-4), 125-133. doi:10.1007/bf01306602 | es_ES |
dc.description.references | Rubio, M. C., Becana, M., Kanematsu, S., Ushimaru, T., & James, E. K. (2009). Immunolocalization of antioxidant enzymes in high-pressure frozen root and stem nodules of Sesbania rostrata. New Phytologist, 183(2), 395-407. doi:10.1111/j.1469-8137.2009.02866.x | es_ES |
dc.description.references | Seregélyes, C., Mustárdy, L., Ayaydin, F., Sass, L., Kovács, L., Endre, G., … Dudits, D. (2000). Nuclear localization of a hypoxia-inducible novel non-symbiotic hemoglobin in cultured alfalfa cells1. FEBS Letters, 482(1-2), 125-130. doi:10.1016/s0014-5793(00)02049-4 | es_ES |
dc.description.references | Smagghe, B. J., Blervacq, A.-S., Blassiau, C., Decottignies, J.-P., Jacquot, J.-P., Hargrove, M. S., & Hilbert, J.-L. (2007). Immunolocalization of Non-Symbiotic Hemoglobins During Somatic Embryogenesis in Chicory. Plant Signaling & Behavior, 2(1), 43-49. doi:10.4161/psb.2.1.3812 | es_ES |
dc.description.references | Smagghe, B. J., Hoy, J. A., Percifield, R., Kundu, S., Hargrove, M. S., Sarath, G., … Appleby, C. A. (2009). Review: Correlations between oxygen affinity and sequence classifications of plant hemoglobins. Biopolymers, 91(12), 1083-1096. doi:10.1002/bip.21256 | es_ES |
dc.description.references | Spyrakis, F., Bruno, S., Bidon-Chanal, A., Luque, F. J., Abbruzzetti, S., Viappiani, C., … Mozzarelli, A. (2011). Oxygen binding to Arabidopsis thaliana AHb2 nonsymbiotic hemoglobin: evidence for a role in oxygen transport. IUBMB Life, 63(5), 355-362. doi:10.1002/iub.470 | es_ES |
dc.description.references | Sturms, R., Kakar, S., Trent, J., & Hargrove, M. S. (2010). TremaandParasponiaHemoglobins Reveal Convergent Evolution of Oxygen Transport in Plants. Biochemistry, 49(19), 4085-4093. doi:10.1021/bi1002844 | es_ES |
dc.description.references | Taylor, E. R., Nie, X. Z., MacGregor, A. W., & Hill, R. D. (1994). A cereal haemoglobin gene is expressed in seed and root tissues under anaerobic conditions. Plant Molecular Biology, 24(6), 853-862. doi:10.1007/bf00014440 | es_ES |
dc.description.references | Trent, J. T., Watts, R. A., & Hargrove, M. S. (2001). Human Neuroglobin, a Hexacoordinate Hemoglobin That Reversibly Binds Oxygen. Journal of Biological Chemistry, 276(32), 30106-30110. doi:10.1074/jbc.c100300200 | es_ES |
dc.description.references | Trevaskis, B., Watts, R. A., Andersson, C. R., Llewellyn, D. J., Hargrove, M. S., Olson, J. S., … Peacock, W. J. (1997). Two hemoglobin genes in Arabidopsis thaliana: The evolutionary origins of leghemoglobins. Proceedings of the National Academy of Sciences, 94(22), 12230-12234. doi:10.1073/pnas.94.22.12230 | es_ES |
dc.description.references | Uchiumi, T., Shimoda, Y., Tsuruta, T., Mukoyoshi, Y., Suzuki, A., Senoo, K., … Abe, M. (2002). Expression of Symbiotic and Nonsymbiotic Globin Genes Responding to Microsymbionts on Lotus japonicus. Plant and Cell Physiology, 43(11), 1351-1358. doi:10.1093/pcp/pcf165 | es_ES |
dc.description.references | Vieweg, M. F., Hohnjec, N., & K�ster, H. (2004). Two genes encoding different truncated hemoglobins are regulated during root nodule and arbuscular mycorrhiza symbioses of Medicago truncatula. Planta, 220(5), 757-766. doi:10.1007/s00425-004-1397-0 | es_ES |
dc.description.references | Vigeolas, H., Hühn, D., & Geigenberger, P. (2011). Nonsymbiotic Hemoglobin-2 Leads to an Elevated Energy State and to a Combined Increase in Polyunsaturated Fatty Acids and Total Oil Content When Overexpressed in Developing Seeds of Transgenic Arabidopsis Plants. Plant Physiology, 155(3), 1435-1444. doi:10.1104/pp.110.166462 | es_ES |
dc.description.references | Vinogradov, S. N., Hoogewijs, D., Bailly, X., Arredondo-Peter, R., Guertin, M., Gough, J., … Vanfleteren, J. R. (2005). Three globin lineages belonging to two structural classes in genomes from the three kingdoms of life. Proceedings of the National Academy of Sciences, 102(32), 11385-11389. doi:10.1073/pnas.0502103102 | es_ES |
dc.description.references | Wang, Y., Elhiti, M., Hebelstrup, K. H., Hill, R. D., & Stasolla, C. (2011). Manipulation of hemoglobin expression affects Arabidopsis shoot organogenesis. Plant Physiology and Biochemistry, 49(10), 1108-1116. doi:10.1016/j.plaphy.2011.06.005 | es_ES |
dc.description.references | Watts, R. A., Hunt, P. W., Hvitved, A. N., Hargrove, M. S., Peacock, W. J., & Dennis, E. S. (2001). A hemoglobin from plants homologous to truncated hemoglobins of microorganisms. Proceedings of the National Academy of Sciences, 98(18), 10119-10124. doi:10.1073/pnas.191349198 | es_ES |
dc.description.references | Weber, R. E., & Vinogradov, S. N. (2001). Nonvertebrate Hemoglobins: Functions and Molecular Adaptations. Physiological Reviews, 81(2), 569-628. doi:10.1152/physrev.2001.81.2.569 | es_ES |
dc.description.references | Zhang, L., Onda, K., Imai, R., Fukuda, R., Horiuchi, H., & Ohta, A. (2003). Growth temperature downshift induces antioxidant response in Saccharomyces cerevisiae. Biochemical and Biophysical Research Communications, 307(2), 308-314. doi:10.1016/s0006-291x(03)01168-9 | es_ES |