Sabarinathan K Gopalasubramaniam, Kalyan C Kondapalli, César Millán-Pacheco, Nina Pastor, Timothy L Stemmler, Jose F Moran, Raúl Arredondo-Peter
{"title":"大豆二氢脂酰胺脱氢酶(铁血红蛋白还原酶2)与铁水稻非共生血红蛋白1相互作用并降低。","authors":"Sabarinathan K Gopalasubramaniam, Kalyan C Kondapalli, César Millán-Pacheco, Nina Pastor, Timothy L Stemmler, Jose F Moran, Raúl Arredondo-Peter","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>Ferrous oxygenated hemoglobins (Hb<sup>2+</sup>O<sub>2</sub>) autoxidize to ferric Hb<sup>3+</sup>, but Hb<sup>3+</sup> is reduced to Hb<sup>2+</sup> by enzymatic and non-enzymatic mechanisms. We characterized the interaction between the soybean ferric leghemoglobin reductase 2 (FLbR2) and ferric rice non-symbiotic Hb1 (Hb1<sup>3+</sup>). Spectroscopic analysis showed that FLbR2 reduces Hb1<sup>3+</sup>. Analysis by tryptophan fluorescence quenching showed that FLbR2 interacts with Hb1<sup>3+</sup>, however the use of ITC and IEF techniques revealed that this interaction is weak. <i>In silico</i> modeling showed that predicted FLbR2 and native Hb1<sup>3+</sup> interact at the FAD-binding domain of FLbR2 and the CD-loop and helix F of Hb1<sup>3+</sup>.</p>","PeriodicalId":90724,"journal":{"name":"Sciencejet","volume":"2 ","pages":""},"PeriodicalIF":0.0000,"publicationDate":"2013-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4243682/pdf/nihms601276.pdf","citationCount":"0","resultStr":"{\"title\":\"Soybean dihydrolipoamide dehydrogenase (ferric leghemoglobin reductase 2) interacts with and reduces ferric rice non-symbiotic hemoglobin 1.\",\"authors\":\"Sabarinathan K Gopalasubramaniam, Kalyan C Kondapalli, César Millán-Pacheco, Nina Pastor, Timothy L Stemmler, Jose F Moran, Raúl Arredondo-Peter\",\"doi\":\"\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Ferrous oxygenated hemoglobins (Hb<sup>2+</sup>O<sub>2</sub>) autoxidize to ferric Hb<sup>3+</sup>, but Hb<sup>3+</sup> is reduced to Hb<sup>2+</sup> by enzymatic and non-enzymatic mechanisms. We characterized the interaction between the soybean ferric leghemoglobin reductase 2 (FLbR2) and ferric rice non-symbiotic Hb1 (Hb1<sup>3+</sup>). Spectroscopic analysis showed that FLbR2 reduces Hb1<sup>3+</sup>. Analysis by tryptophan fluorescence quenching showed that FLbR2 interacts with Hb1<sup>3+</sup>, however the use of ITC and IEF techniques revealed that this interaction is weak. <i>In silico</i> modeling showed that predicted FLbR2 and native Hb1<sup>3+</sup> interact at the FAD-binding domain of FLbR2 and the CD-loop and helix F of Hb1<sup>3+</sup>.</p>\",\"PeriodicalId\":90724,\"journal\":{\"name\":\"Sciencejet\",\"volume\":\"2 \",\"pages\":\"\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2013-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4243682/pdf/nihms601276.pdf\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Sciencejet\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Sciencejet","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Soybean dihydrolipoamide dehydrogenase (ferric leghemoglobin reductase 2) interacts with and reduces ferric rice non-symbiotic hemoglobin 1.
Ferrous oxygenated hemoglobins (Hb2+O2) autoxidize to ferric Hb3+, but Hb3+ is reduced to Hb2+ by enzymatic and non-enzymatic mechanisms. We characterized the interaction between the soybean ferric leghemoglobin reductase 2 (FLbR2) and ferric rice non-symbiotic Hb1 (Hb13+). Spectroscopic analysis showed that FLbR2 reduces Hb13+. Analysis by tryptophan fluorescence quenching showed that FLbR2 interacts with Hb13+, however the use of ITC and IEF techniques revealed that this interaction is weak. In silico modeling showed that predicted FLbR2 and native Hb13+ interact at the FAD-binding domain of FLbR2 and the CD-loop and helix F of Hb13+.