高等研究院 Institute for Advanced Study
Structural Studies of Mammalian
Respiratory Complex I
Dr. Jiapeng Zhu, Ph.D.
University of Illinois at Urbana-Champaign
About the speaker
Dr. Jiapeng Zhu did his Ph.D. program at the University of Illinois at Urbana-Champaign, USA, and pursued his thesis research on the highly challenging membrane protein cytochrome c oxidase from bacteria, under the guidance of Prof. Robert Gennis in Department of Biochemistry. Following his Ph.D., Dr. Zhu obtained a position in Dr. Judy Hirst’s lab at the MRC Mitochondrial Biology Unit as a Career Development Fellow. Here, he worked on one of the most challenging projects in structural biology - bovine heart complex I.
NADH:ubiquinone oxidoreductase (complex I), the entry enzyme of the respiratory chain, transfers electrons from the NADH substrate to ubiquinone through a pathway containing a flavin and a series of iron-sulfur clusters. Furthermore, using the excess energy of NADH oxidation, complex I pumps protons against their concentration gradient across the membrane and conserves it in a proton motive force that can be utilized for ATP synthesis. The complex I from bovine heart comprises 14 core subunits, corresponding to the minimal complex I found in eubacteria, and 30 supernumerary subunits which are specific to the mammalian enzyme. The bovine enzyme serves as a good model for human complex I owing to their high degree of homology. The bovine heart complex I was purified and studied with x-ray crystallography and single-particle electron cryo-microscopy, and a 5 Å resolution EM map of the intact enzyme, and a 7 Å resolution x-ray diffraction data of the membrane arm subcomplex were obtained. The analysis of these data considerably advanced the knowledge of the 3-dimensional structure of mammalian complex I.
时间: 2015年4月29日 上午09:30-10:30
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