dc.creator | Lopez Rivero, Arleth Susana | |
dc.creator | Rossi, María Agustina | |
dc.creator | Ceccarelli, Eduardo Augusto | |
dc.creator | Catalano Dupuy, Daniela Luján | |
dc.date.accessioned | 2022-03-16T01:53:01Z | |
dc.date.accessioned | 2022-10-14T22:32:55Z | |
dc.date.available | 2022-03-16T01:53:01Z | |
dc.date.available | 2022-10-14T22:32:55Z | |
dc.date.created | 2022-03-16T01:53:01Z | |
dc.date.issued | 2019-04 | |
dc.identifier | Lopez Rivero, Arleth Susana; Rossi, María Agustina; Ceccarelli, Eduardo Augusto; Catalano Dupuy, Daniela Luján; A bacterial 2[4Fe–4S] ferredoxin as redox partner of the plastidic-type ferredoxin-NADP + reductase from Leptospira interrogans; Elsevier Science; Biochimica et Biophysica Acta - General Subjects; 1863; 4; 4-2019; 651-660 | |
dc.identifier | 0304-4165 | |
dc.identifier | http://hdl.handle.net/11336/153417 | |
dc.identifier | CONICET Digital | |
dc.identifier | CONICET | |
dc.identifier.uri | https://repositorioslatinoamericanos.uchile.cl/handle/2250/4314449 | |
dc.description.abstract | Background: Ferredoxins are small iron-sulfur proteins that participate as electron donors in various metabolic pathways. They are recognized substrates of ferredoxin-NADP + reductases (FNR) in redox metabolisms in mitochondria, plastids, and bacteria. We previously found a plastidic-type FNR in Leptospira interrogans (LepFNR), a parasitic bacterium of animals and humans. Nevertheless, we did not identify plant-type ferredoxins or flavodoxins, the common partners of this kind of FNR. Methods: Sequence alignment, phylogenetical analyses and structural modeling were performed for the identification of a 2[4Fe–4S] ferredoxin (LepFd2) as a putative redox partner of LepFNR in L. interrogans. The gene encoding LepFd2 was cloned and the protein overexpressed and purified. The functional properties of LepFd2 and LepFNR-LepFd2 complex were analyzed by kinetic and mutagenesis studies. Results: We succeeded in expressing and purifying LepFd2 with its Fe–S cluster properly bound. We found that LepFd2 exchanges electrons with LepFNR. Moreover, a unique structural subdomain of LepFNR (loop P75-Y91), was shown to be involved in the recognition and binding of LepFd2. This structural subdomain is not found in other FNR homologs. Conclusions: We report for the first time a redox pair in L. interrogans in which a plastidic FNR exchanges electron with a bacterial 2[4Fe–4S] ferredoxin. We characterized this reaction and proposed a model for the productive LepFNR-LepFd2 complex. General significance: Our findings suggest that the interaction of LepFNR with the iron-sulfur protein would be different from the one previously described for the homolog enzymes. This knowledge would be useful for the design of specific LepFNR inhibitors. | |
dc.language | eng | |
dc.publisher | Elsevier Science | |
dc.relation | info:eu-repo/semantics/altIdentifier/url/https://linkinghub.elsevier.com/retrieve/pii/S0304416519300042 | |
dc.relation | info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/j.bbagen.2019.01.004 | |
dc.rights | https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ | |
dc.rights | info:eu-repo/semantics/openAccess | |
dc.subject | FERREDOXIN | |
dc.subject | FERREDOXIN-NADP+REDUCTASE | |
dc.subject | IRON-SULFUR CLUSTERS | |
dc.subject | LEPTOSPIRA INTERROGANS | |
dc.title | A bacterial 2[4Fe–4S] ferredoxin as redox partner of the plastidic-type ferredoxin-NADP + reductase from Leptospira interrogans | |
dc.type | info:eu-repo/semantics/article | |
dc.type | info:ar-repo/semantics/artículo | |
dc.type | info:eu-repo/semantics/publishedVersion | |