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    Home > Biochemistry News > Biotechnology News > Chlorophyll synthesis key enzyme crystal structure revealed for the first time

    Chlorophyll synthesis key enzyme crystal structure revealed for the first time

    • Last Update: 2020-06-07
    • Source: Internet
    • Author: User
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    "Everything grows by the sun", light-dependent protochlorophytine stepothesin, is essential for the growth and development of green plantsAlthough it has been nearly 100 years since the discovery of this key enzyme, scientists have been unable to demystify its protein structureCheng Qi Team and Shanghai Jiaotong University University' Ph.DTeam, Team Nigel Scruton, Ph.Dof the Institute of Biotechnology, University of Manchester, United Kingdom, found the crystal structure of light-dependent provost acid stenosin stenosin monomer, light-dependent provostacid acid oxidant stenosin acid acid acid polygon acidphosphate complexThe clarification of crystal structure and the precision modeling of its terlith complex reveal how the relevant active sites can carry out local hydrogenation transfer and long-range proton transfer along the proton transfer path defined by the structure, promoting the reduction of primary chlorophyll driven by light" study provides a critical missing link between the enzyme protein structure and excitation state chemistry, which is important for the engineering design of photocatalytic chemical and biological catalysts and related protein small molecule inhibitorsCheng Qi, co-author of the study, said the work also paves the way for detailed computational analysis of the quantitative light-to-chemical conversion response, and that a more complete description of the catalytic effect is a major challenge in enzymaticsthe results of the study, co-author Sun Wenli, Ph.D., Institute of Biotechnology, Chinese Academy of Agricultural Sciences, said the study will help to further improve the evolution of some of the key enzyme proteins in the process of convergence evolution and the future predictability directionit is learned that the results fill the gap in the three-dimensional crystal structure of photosynthesis biosynthetic photosynthetic photosynthetic enzymes and their cofactor complexes in the past 100 years, and have a landmark significance.
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