Gell David A
School of Medicine, University of Tasmania, TAS 7000, Australia.
Blood Cells Mol Dis. 2018 May;70:13-42. doi: 10.1016/j.bcmd.2017.10.006. Epub 2017 Oct 31.
Haemoglobin (Hb) is widely known as the iron-containing protein in blood that is essential for O transport in mammals. Less widely recognised is that erythrocyte Hb belongs to a large family of Hb proteins with members distributed across all three domains of life-bacteria, archaea and eukaryotes. This review, aimed chiefly at researchers new to the field, attempts a broad overview of the diversity, and common features, in Hb structure and function. Topics include structural and functional classification of Hbs; principles of O binding affinity and selectivity between O/NO/CO and other small ligands; hexacoordinate (containing bis-imidazole coordinated haem) Hbs; bacterial truncated Hbs; flavohaemoglobins; enzymatic reactions of Hbs with bioactive gases, particularly NO, and protection from nitrosative stress; and, sensor Hbs. A final section sketches the evolution of work on the structural basis for allosteric O binding by mammalian RBC Hb, including the development of newer kinetic models. Where possible, reference to historical works is included, in order to provide context for current advances in Hb research.
血红蛋白（Hb）作为血液中含有的蛋白质广为人知，它对于哺乳动物体内氧气的运输至关重要。红细胞血红蛋白属于一个庞大的血红蛋白蛋白质家族，其成员分布在生命的所有三个领域——细菌、古细菌和真核生物中，但这一点鲜为人知。本综述主要面向该领域的新手研究人员，试图对血红蛋白结构和功能的多样性及共同特征进行广泛概述。主题包括血红蛋白的结构和功能分类；氧气结合亲和力以及氧气/一氧化氮/一氧化碳与其他小分子配体之间选择性的原理；六配位（含双咪唑配位血红素）血红蛋白；细菌截短型血红蛋白；黄素血红蛋白；血红蛋白与生物活性气体（特别是一氧化氮）的酶促反应以及免受亚硝化应激的影响；还有传感血红蛋白。最后一部分概述了关于哺乳动物红细胞血红蛋白变构氧结合结构基础的研究进展，包括更新的动力学模型的发展。在可能的情况下，还会提及历史著作，以便为血红蛋白研究的当前进展提供背景信息。
