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Tan Kah Kee Science Award in Life Sciences 2006

Rao Zihe, biophysicist, was born on 6 September, 1950 in Nanjing, Jiangsu province. He graduated with a major in Biophysics from the University of Science and Technology of China (USTC) in 1977; he gained his Master’s degree from the graduate school of the Chinese Academy of Sciences in 1982; he obtained his PhD from Melbourne University in 1989. He was engaged in research in the Laboratory of Molecular Biophysics, University of Oxford from 1989-1996. He is a member of the Chinese Academy of Sciences, a member of the Third World Academy of Science. and a professor of Tsinghua University. He is currently holds the positions of Director-general of the Institute of Biophysics, Chinese Academy of Sciences and Director of the National Key Laboratory of Biomacromolecules.

Rao Zihe is mainly involved in research on the structure and function of important virus and tumor related proteins, as well as protein engineering and innovative drug discovery. A total of 159 papers have already been published in internationally renowned journals such as CellNatureNature Structural & Molecular BiologyPLoS Biology, PNASJ Biol. Chem.StructureJ. Mol. Biol.J Am Chem. Soc., and Curr. Opin. Struct. Biol.
 
 
 
Crystal Structure of Mitochondrial Respiratory Membrane Protein Complex II
Abstract
The mitochondrial respiratory Complex II or succinate:ubiquinone oxidoreductase (SQR) is an integral membrane protein complex in both the tricarboxylic acid cycle and aerobic respiration. Here it reports the first crystal structure of Complex II from porcine heart at 2.4 ?resolution and its complex structure with inhibitors 3-nitropropionate and 2-thenoyltrifluoroacetone (TTFA) at 3.5 ?resolution. Complex II comprises of two hydrophilic proteins, flavoprotein (Fp) and iron-sulfur protein (Ip), and two trans-membrane proteins (CybL and CybS), as well as prosthetic groups required for electron transfer from succinate to ubiquinone. The structure correlates the protein environments around prosthetic groups with their unique midpoint redox potentials. Two ubiquinone binding sites are discussed and elucidated by TTFA binding. The Complex II structure provides a bona fide model for study of the mitochondrial respiratory system and human mitochondrial diseases related to mutations in this complex.