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Soybean dihydrolipoamide dehydrogenase (ferric leghemoglobin reductase 2) interacts with and reduces ferric rice non-symbiotic hemoglobin 1.


ABSTRACT: 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+.

SUBMITTER: Gopalasubramaniam SK 

PROVIDER: S-EPMC4243682 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature

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Soybean dihydrolipoamide dehydrogenase (ferric leghemoglobin reductase 2) interacts with and reduces ferric rice non-symbiotic hemoglobin 1.

Gopalasubramaniam Sabarinathan K SK   Kondapalli Kalyan C KC   Millán-Pacheco César C   Pastor Nina N   Stemmler Timothy L TL   Moran Jose F JF   Arredondo-Peter Raúl R  

Sciencejet 20130101


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+</s  ...[more]

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