SAXS structure of homodimeric oxyHemoglobin III from bivalve Lucina pectinata,Biopolymers

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SAXS structure of homodimeric oxyHemoglobin III from bivalve Lucina pectinata
Biopolymers ( IF 3.2 ) Pub Date : 2021-04-01 , DOI: 10.1002/bip.23427
Darya Marchany-Rivera ₁ , Rafael A Estremera-Andújar ₂ , Carlos Nieves-Marrero ₂ , Carlos R Ruiz-Martínez ₂ , William Bauer ₃ , Juan López-Garriga ₁

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Hemoglobin III (HbIII) is one of the two oxygen reactive hemoproteins present in the bivalve, Lucina pectinata. The clam inhabits a sulfur-rich environment and HbIII is the only hemoprotein present in the system which does not yet have a structure described elsewhere. It is known that HbIII exists as a heterodimer with hemoglobin II (HbII) to generate the stable Oxy(HbII-HbIII) complex but it remains unknown if HbIII can form a homodimeric species. Here, a new chromatographic methodology to separate OxyHbIII from the HbII-HbIII dimer has been developed, employing a fast performance liquid chromatography and ionic exchange chromatography column. The nature of OxyHbIII in solution at concentrations from 1.6 mg/mL to 20.4 mg/mL was studied using small angle X-ray scattering (SAXS). The results show that at all concentrations, the Oxy(HbIII-HbIII) dimer dominates in solution. However, as the concentration increases to nonphysiological values, 20.4 mg/mL, HbIII forms a 30% tetrameric fraction. Thus, there is a direct relationship between the Oxy(HbIII-HbIII) oligomeric form and hemoglobin concentration. We suggest it is likely that the OxyHbIII dimer contributes to active oxygen transport in tissues of L pectinata, where the Oxy(HbII-HbIII) complex is not present.

中文翻译：

双壳类 Lucina pectinata 同源二聚体氧合血红蛋白 III 的 SAXS 结构

血红蛋白 III (HbIII) 是双壳贝类Lucina pectinata中存在的两种氧反应性血红蛋白之一. 蛤蜊栖息在富含硫的环境中，HbIII 是系统中唯一存在的血红蛋白，它还没有其他地方描述的结构。已知 HbIII 与血红蛋白 II (HbII) 以异二聚体形式存在，以生成稳定的 Oxy(HbII-HbIII) 复合物，但 HbIII 是否可以形成同源二聚体物种仍然未知。在这里，已经开发出一种新的色谱方法，使用快速高效液相色谱和离子交换色谱柱从 HbII-HbIII 二聚体中分离 OxyHbIII。使用小角 X 射线散射 (SAXS) 研究了溶液中浓度为 1.6 mg/mL 至 20.4 mg/mL 的 OxyHbIII 的性质。结果表明，在所有浓度下，Oxy(HbIII-HbIII) 二聚体在溶液中占主导地位。然而，随着浓度增加到非生理值，20.4 mg/mL，HbIII 形成 30% 的四聚体部分。因此，Oxy(HbIII-HbIII) 寡聚形式与血红蛋白浓度之间存在直接关系。我们认为 OxyHbIII 二聚体可能有助于组织中的活性氧转运。L pectinata，其中不存在 Oxy(HbII-HbIII) 复合物。

更新日期：2021-04-01

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