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Water Promoting Electron Hole Transport between Tyrosine and Cysteine in Proteins via a Special Mechanism: Double Proton Coupled Electron Transfer
來源:陳效華教授個人網(wǎng)站 發(fā)布日期:2016-04-04
作者:Xiaohua Chen*, Guangcai Ma, Weichao Sun, Hongjing Dai, Dong Xiao, Yanfang Zhang, Xin Qin, Yongjun Li
關(guān)鍵字:Tyrosine; Cysteine; Double Proton Coupled Electron Transfer
論文來源:期刊
具體來源:J. Am. Chem. Soc., 2014, 136 (12), pp 4515–4524
發(fā)表時間:2014年
The proton/electron transfer reactions between cysteine residue (Cys) and tyrosinyl radical (Tyr?) are an important step for many enzyme-catalyzed processes. On the basis of the statistical analysis of protein data bank, we designed three representative models to explore the possible proton/electron transfer mechanisms from Cys to Tyr? in proteins. Our ab initio calculations on simplified models and quantum mechanical/molecular mechanical (QM/MM) calculations on real protein environment reveal that the direct electron transfer between Cys and Tyr? is difficult to occur, but an inserted water molecule can greatly promote the proton/electron transfer reactions by a double-proton-coupled electron transfer (dPCET) mechanism. The inserted H2O plays two assistant roles in these reactions. The first one is to bridge the side chains of Tyr? and Cys via two hydrogen bonds, which act as the proton pathway, and the other one is to enhance the electron overlap between the lone-pair orbital of sulfur atom and the π-orbital of phenol moiety and to function as electron transfer pathway. This water-mediated dPCET mechanism may offer great help to understand the detailed electron transfer processes between Tyr and Cys residues in proteins, such as the electron transfer from Cys439 to Tyr730? in the class I ribonucleotide reductase.
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