化学
亚硫酸盐
亚硫酸盐还原酶
血红素
酶
辅因子
组合化学
生物催化
硫黄
还原酶
蛋白质工程
催化作用
生物化学
立体化学
有机化学
反应机理
作者
Evan N. Mirts,Igor D. Petrik,Parisa Hosseinzadeh,Mark J. Nilges,Yi Lu
出处
期刊:Science
[American Association for the Advancement of Science (AAAS)]
日期:2018-09-14
卷期号:361 (6407): 1098-1101
被引量:110
标识
DOI:10.1126/science.aat8474
摘要
Metals brought together do more Enzymatic reduction of oxyanions such as sulfite (SO 3 2− ) requires the delivery of multiple electrons and protons, a feat accomplished by cofactors tailored for catalysis and electron transport. Replicating this strategy in protein scaffolds may expand the range of enzymes that can be designed de novo. Mirts et al. selected a scaffold protein containing a natural heme cofactor and then engineered a cavity suitable for binding a second cofactor—an iron-sulfur cluster (see the Perspective by Lancaster). The resulting designed enzyme was optimized through rational mutation into a catalyst with spectral characteristics and activity similar to that of natural sulfite reductases. Science , this issue p. 1098 ; see also p. 1071
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