Hemoglobin wonders: a fascinating gas transporter dive into molluscs.

IF 6.2 2区 生物学 Q1 BIOCHEMISTRY & MOLECULAR BIOLOGY
Weifeng Zhang, Yang Zhang, Xizhi Shi, Shi Wang, Yongbo Bao
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引用次数: 0

Abstract

Hemoglobin (Hb) has been identified in at least 14 molluscan taxa so far. Research spanning over 130 years on molluscan Hbs focuses on their genes, protein structures, functions, and evolution. Molluscan Hbs are categorized into single-, two-, and multiple-domain chains, including red blood cell, gill, and extracellular Hbs, based on the number of globin domains and their respective locations. These Hbs exhibit variation in assembly, ranging from monomeric and dimeric to higher-order multimeric forms. Typically, molluscan Hbs display moderately high oxygen affinity, weak cooperativity, and varying pH sensitivity. Hb's potential role in antimicrobial pathways could augment the immune defense of bivalves, which may be a complement to their lack of adaptive immunity. The role of Hb as a respiratory protein in bivalves likely originated from the substitution of hemocyanin. Molluscan Hbs demonstrate adaptive evolution in response to environmental changes via various strategies (e.g. increasing Hb types, multimerization, and amino acid residue substitutions at key sites), enhancing or altering functional properties for habitat adaptation. Concurrently, an increase in Hb assembly diversity, coupled with a downward trend in oxygen affinity, is observed during molluscan differentiation and evolution. Hb in Protobranchia, Heteroconchia, and Pteriomorphia bivalves originated from separate ancestors, with Protobranchia inheriting a relative ancient molluscan Hb gene. In bivalves, extracellular Hbs share a common origin, while gill Hbs likely emerged from convergent evolution. In summary, research on molluscan Hbs offers valuable insights into the origins, biological variations, and adaptive evolution of animal Hbs.

血红蛋白奇观:软体动物中令人着迷的气体运输工具。
迄今为止,至少在 14 个软体动物类群中发现了血红蛋白(Hb)。关于软体动物血红蛋白的研究历时 130 多年,主要集中在其基因、蛋白质结构、功能和进化方面。根据球蛋白结构域的数量和各自的位置,软体动物球蛋白可分为单链、双链和多链,包括红细胞球蛋白、鳃球蛋白和细胞外球蛋白。这些 Hbs 的组装方式各不相同,有单体和二聚体,也有更高级的多聚体形式。通常,软体动物的 Hbs 具有中等程度的高氧亲和性、弱合作性和不同的 pH 敏感性。Hb 在抗菌途径中的潜在作用可以增强双壳类动物的免疫防御能力,这可能是对它们缺乏适应性免疫的一种补充。Hb 在双壳类动物中作为呼吸蛋白的作用可能源于血蓝蛋白的替代。软体动物的 Hbs 通过各种策略(如增加 Hb 类型、多聚化和关键位点的氨基酸残基替代)表现出适应环境变化的进化,增强或改变功能特性以适应栖息地。与此同时,在软体动物的分化和进化过程中,还观察到 Hb 组装多样性的增加以及氧亲和性的下降趋势。双壳类原枝藻、异形藻和翼手目中的 Hb 起源于不同的祖先,其中原枝藻继承了一个相对古老的软体动物 Hb 基因。在双壳类中,细胞外 Hbs 有着共同的起源,而鳃 Hbs 很可能是趋同进化产生的。总之,对软体动物 Hbs 的研究为了解动物 Hbs 的起源、生物变异和适应性进化提供了宝贵的信息。
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来源期刊
CiteScore
14.90
自引率
0.00%
发文量
6
期刊介绍: As the discipline of biochemistry and molecular biology have greatly advanced in the last quarter century, significant contributions have been made towards the advancement of general medicine, genetics, immunology, developmental biology, and biophysics. Investigators in a wide range of disciplines increasingly require an appreciation of the significance of current biochemical and molecular biology advances while, members of the biochemical and molecular biology community itself seek concise information on advances in areas remote from their own specialties. Critical Reviews in Biochemistry and Molecular Biology believes that well-written review articles prove an effective device for the integration and meaningful comprehension of vast, often contradictory, literature. Review articles also provide an opportunity for creative scholarship by synthesizing known facts, fruitful hypotheses, and new concepts. Accordingly, Critical Reviews in Biochemistry and Molecular Biology publishes high-quality reviews that organize, evaluate, and present the current status of high-impact, current issues in the area of biochemistry and molecular biology. Topics are selected on the advice of an advisory board of outstanding scientists, who also suggest authors of special competence. The topics chosen are sufficiently broad to interest a wide audience of readers, yet focused enough to be within the competence of a single author. Authors are chosen based on their activity in the field and their proven ability to produce a well-written publication.
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