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。

Sciencejet Pub Date : 2013-01-01
Sabarinathan K Gopalasubramaniam, Kalyan C Kondapalli, César Millán-Pacheco, Nina Pastor, Timothy L Stemmler, Jose F Moran, Raúl Arredondo-Peter
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引用次数: 0

摘要

铁氧合血红蛋白(Hb2+O2)自氧化为铁Hb3+,但Hb3+通过酶和非酶机制还原为Hb2+。我们鉴定了大豆铁血红蛋白还原酶2 (FLbR2)和铁水稻非共生Hb1 (Hb13+)之间的相互作用。光谱分析表明,FLbR2还原Hb13+。色氨酸荧光猝灭分析显示FLbR2与Hb13+相互作用,但ITC和IEF技术显示这种相互作用很弱。计算机模拟显示,预测的FLbR2和天然Hb13+在FLbR2的fad结合域和Hb13+的cd环和螺旋F上相互作用。
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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+.

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Wireless magnetoelastic sensors for tracking degradation profiles of nitrodopamine-modified poly(ethylene glycol). Soybean dihydrolipoamide dehydrogenase (ferric leghemoglobin reductase 2) interacts with and reduces ferric rice non-symbiotic hemoglobin 1.
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