Lin Ying-Wu
School of Chemistry and Chemical Engineering, University of South China, Hengyang 421001, China; Laboratory of Protein Structure and Function, University of South China, Hengyang 421001, China.
Biochim Biophys Acta. 2015 Aug;1854(8):844-59. doi: 10.1016/j.bbapap.2015.04.019. Epub 2015 Apr 24.
Heme proteins perform a large array of biological functions using the same heme cofactor. A primary method of regulating these diverse functions is the heme-protein cross-link, an important post-translational modification. This review presents an overview of the broad diversity of heme-protein cross-links, including Cys/SeCys -heme, Met-heme, His-heme, Trp/Tyr-heme, Glu/Asp-heme and Lys-heme cross-links, which have been discovered in the last three decades, with bond type ranging from C-S, C-Se, C-N, C-C to C-O. Many advances have been made in revealing the mechanisms of heme-protein cross-link formation, as well as the structural and functional roles. Moreover, most of these cross-links have been successfully recreated in natural or de novo proteins. These tremendous progresses have not only enhanced our knowledge of how cross-links fine-tune the structure and function of natural heme proteins, but also provided us powerful strategies for design of artificial heme proteins with functionalities beyond those of natural heme proteins.
血红素蛋白利用相同的血红素辅因子执行大量的生物学功能。调节这些多样功能的一种主要方法是血红素-蛋白质交联，这是一种重要的翻译后修饰。本综述概述了血红素-蛋白质交联的广泛多样性，包括过去三十年中发现的半胱氨酸/硒代半胱氨酸-血红素、甲硫氨酸-血红素、组氨酸-血红素、色氨酸/酪氨酸-血红素、谷氨酸/天冬氨酸-血红素和赖氨酸-血红素交联，其键型从C-S、C-Se、C-N、C-C到C-O。在揭示血红素-蛋白质交联形成的机制以及结构和功能作用方面已经取得了许多进展。此外，这些交联中的大多数已经在天然或从头合成的蛋白质中成功重现。这些巨大的进展不仅增强了我们对交联如何微调天然血红素蛋白的结构和功能的认识，也为设计具有超越天然血红素蛋白功能的人工血红素蛋白提供了有力策略。
