Department of Chemistry, University of Michigan, Ann Arbor, Michigan 48109 United States.
Chem Rev. 2022 Jul 27;122(14):12046-12109. doi: 10.1021/acs.chemrev.1c01025. Epub 2022 Jun 28.
One of the hallmark advances in our understanding of metalloprotein function is showcased in our ability to design new, non-native, catalytically active protein scaffolds. This review highlights progress and milestone achievements in the field of metalloprotein design focused on reports from the past decade with special emphasis on designs couched within common subfields of bioinorganic study: heme binding proteins, monometal- and dimetal-containing catalytic sites, and metal-containing electron transfer sites. Within each subfield, we highlight several of what we have identified as significant and important contributions to either our understanding of that subfield or metalloprotein design as a discipline. These reports are placed in context both historically and scientifically. General suggestions for future directions that we feel will be important to advance our understanding or accelerate discovery are discussed.
我们对金属蛋白酶功能的理解取得了标志性的进展之一，体现在我们能够设计新的、非天然的、具有催化活性的蛋白质支架上。这篇综述重点介绍了过去十年中金属蛋白酶设计领域的进展和里程碑式成就，特别强调了生物无机研究常见子领域内的设计：血红素结合蛋白、单金属和双金属催化位点以及含金属的电子转移位点。在每个子领域中，我们重点介绍了一些我们认为对该子领域或金属蛋白酶设计作为一个学科的理解具有重要意义和重要贡献的内容。这些报告从历史和科学的角度进行了背景分析。讨论了我们认为对于推进我们的理解或加速发现将很重要的未来方向的一般性建议。
