Rational Heme Protein Design: All Roads Lead to Rome |
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Authors: | Prof Dr Ying‐Wu Lin Dr Elizabeth B Sawyer Prof Dr Jiangyun Wang |
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Institution: | 1. School of Chemistry and Chemical Engineering, University of South China, Hengyang 421001 (China);2. National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Chaoyang District, Beijing, 100101 (China);3. Laboratory of Noncoding RNA, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Chaoyang District, Beijing 100101 (China) |
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Abstract: | Heme proteins are among the most abundant and important metalloproteins, exerting diverse biological functions including oxygen transport, small molecule sensing, selective C? H bond activation, nitrite reduction, and electron transfer. Rational heme protein designs focus on the modification of the heme‐binding active site and the heme group, protein hybridization and domain swapping, and de novo design. These strategies not only provide us with unique advantages for illustrating the structure–property–reactivity–function (SPRF) relationship of heme proteins in nature but also endow us with the ability to create novel biocatalysts and biosensors. |
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Keywords: | heme proteins metalloporphyrin metalloproteins protein design unnatural amino acids |
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