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Surprising differences in the respiratory protein of insects: A spectroscopic study of haemoglobin from the European honeybee and the malaria mosquito.
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics ( IF 3.2 ) Pub Date : 2020-03-13 , DOI: 10.1016/j.bbapap.2020.140413
Kevin Nys 1 , Bert Cuypers 1 , Herald Berghmans 2 , Dietmar Hammerschmid 2 , Luc Moens 2 , Sylvia Dewilde 2 , Sabine Van Doorslaer 1
Affiliation  

Only recently it was discovered that haemoglobin (Hb) belongs to the standard gene repertoire of insects, although their tracheal system is used for respiration. A classical oxygen-carrying function of Hb is only obvious for hexapods living in hypoxic environments. In other insect species, including the common fruit fly Drosophila melanogaster, the physiological role of Hb is yet unclear. Here, we study recombinant haemoglobin from the European honeybee Apis mellifera (Ame) and the malaria mosquito Anopheles gambiae (Aga). Spectroscopic evidence shows that both proteins can be classified as hexacoordinate Hbs with a strong affinity for the distal histidine. AgaHb1 is proposed to play a role in oxygen transport or sensing based on its multimeric state, slow autoxidation, and small but significant amount of five-coordinated haem in the deoxy ferrous form. AmeHb appears to behave more like vertebrate neuroglobin with a complex function given its diversified distribution in the genome.



中文翻译:

昆虫呼吸蛋白的惊人差异:来自欧洲蜜蜂和疟疾蚊子的血红蛋白的光谱研究。

直到最近才发现血红蛋白(Hb)属于昆虫的标准基因库,尽管它们的气管系统用于呼吸。Hb的经典携氧功能仅对于生活在低氧环境中的六足动物很明显。在其他昆虫物种中,包括常见的果蝇果蝇Drosophila melanogaster),Hb的生理作用尚不清楚。在这里,我们研究了来自欧洲蜜蜂Apis mellifera(Ame)和疟疾蚊子冈比亚按蚊(Aga)的重组血红蛋白。光谱学证据表明,这两种蛋白都可以归类为对远端组氨酸具有强亲和力的六配位Hb。阿加Hb1的多聚体状态,缓慢的自氧化作用以及少量但大量的五价血红素亚铁血红蛋白形式,据认为在氧的转运或传感中起着一定的作用。鉴于其在基因组中的多样化分布,Ame Hb的表现更像具有复杂功能的脊椎动物神经球蛋白。

更新日期:2020-03-19
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