On August 31, Angewandte Chemie published the latest research results of Researcher Wang Jiangyun and Researcher Gong Weimin of the Institute of Biophysics, Chinese Academy of Sciences. This research paper titled Genetic Incorporation of a Metal Chelating Amino Acid as a Probe for Protein Electron Transfer was selected by the magazine as a "very important paper" and an inside cover article.
This study expanded the gene codon to realize the unnatural amino acid 3-pyrazolyl tyrosine encoding metal chelate in living cells, in order to study the phenomenon of photo-induced electron transfer in biological macromolecules, and the use of biological components Controllable photoinduced charge separation provides a powerful tool.
Electron transfer (ET) involves many important biochemical processes in organisms, including photosynthesis. How to transform biological components to achieve efficient and controllable photoinduced charge separation is an important issue and a major bottleneck in the use of synthetic biology to produce renewable energy. At the same time, the current experimental measurement of electron transfer in proteins can usually only be studied by connecting probes to the residues histidine or cysteine ​​contained in the protein itself, so this method can only be used to study small soluble proteins , Limiting its application. The fluorescence quenching caused by light-induced electron transfer (PET) is a powerful tool for exploring dynamic conformational changes in biological macromolecules. However, due to the limitations of current technology, only tyrosine or tryptophan can be used as an electron donor.
In this study, unnatural amino acids with metal chelating ability were inserted into the green fluorescent protein (GFP) by means of gene codon expansion, and for the first time, fast photoinduced electron transfer from the fluorescent center of the fluorescent protein to copper ions was achieved. It was measured that electron transfer occurred within 1 nanosecond (speed near the center of the light). Crystal structure research reveals that 3-pyrazolyl tyrosine has a high-strength binding ability to copper ions.
These new methods provide new research methods for the study of dynamic conformational changes of proteins, new research ideas for the production of renewable energy by means of synthetic biology, and new tools for the design of metal proteins. In this paper, a new viewpoint is proposed that the green fluorescent protein of jellyfish may be the photoreceptor of jellyfish.
Professor Haw Yang, a famous biophysical chemist at Princeton University in the United States, commented: "I believe that unnatural amino acid coding technology will provide researchers in the field of biophysics-protein research with a very valuable tool, and this article is to promote One of the researches developed in this field, because the use of copper as a quencher, can greatly expand the toolkit based on distance measurement. "
Professor GUO Maolin, a famous bioinorganic chemist at the University of Massachusetts, believes that understanding the mechanism of bioelectron transfer has proved to be a challenging and complex scientific issue. Dr. Jiangyun Wang and his colleagues developed a new strategy to study this complex problem by chelating metal ions to unnatural amino acids and encoding them into proteins. They successfully coded the group chelating Cu (II) on the surface of the green fluorescent protein (GFP). Under the light of 405nm, photoinduced electron transfer (PET) occurred rapidly from the protein chromophore to Cu (II). And in one nanosecond to produce reduced copper (I). The beauty of this genetic coding strategy is that it provides opportunities for proteins in living cells to monitor electronic transfer in real time, and this will be even more exciting!
Professor Gao Yiqin, a biophysical chemist at Peking University, said that photoinduced electron transfer is a very useful tool for the study of protein dynamics, but its application is generally limited to relatively simple systems. This work well chelated metal ions to amino acids to proteins, thus providing a new strategy for protein dynamics research. Such a method is likely to significantly improve the applicability of PET in protein kinetics research.
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