PROFILE OF ZOU CHENGLU

Zou Chenglu, Biochemist,  was born in Qingdao,  Shandong Province, in May 1923.  He graduated from Chemistry Department,  National Southwest Associated  University  in Kunming in 1945, and received Ph.  D.  (Biochemistry) of the University of Cambridge, England in 1951. He was professor of the Shanghai Institute of Biochemistry, 1951-1970; research professor of the Institute of Biophysics, 1970-present; Director of the National Laboratory of Biomacromolecules, 1987-1993. Member of the Presidium and Director of the Division of Biology, Chinese Academy of Sciences，1988-1994.
In  the late fifties, Zou was among the first to use partial proteolysis to study the structure-function relation of proteins. He showed that succinate dehydrogenase  is not identical to cytochrome b as believed by many authors at that time and  with Y.L. Wang. He was among the first to purified this enzyme and showed that it has covalently linked FAD as the prosthetic group. He successfully obtained insulin from the reduced A and B chains by oxidation. This paved the way for the total synthesis of bovine insulin which was awarded a National Natural Science Prize, First Class in 1981. He treated the effect of chemical modification of proteins quantitatively and proposed a graphical method for the determination of the number of essential residues in 1962. This has been described in detail in textbooks and monographs. The equations obtained are known as Zou’s equation and the plot as the Zou’s plot.
He pioneered the study on irreversible modification kinetics of enzyme activity and showed that the concept of substrate-inhibitor competition applies to both reversible and irreversible cases. From the equations derived the apparent rate constant for the irreversible modification step can be obtained in one experiment. This method is now widely used and cited in the literature. Based on a series of experimental studies beginning in the early eighties showing that for some enzymes, inactivation takes place before conformational changes can be detected by conventional methods during denaturation, he suggested that enzyme active site is situated in a region more susceptible to perturbations by denaturants and hence more flexible than the molecule as a whole and this flexibility is required for the catalytic activities of the enzymes concerned. Recently, he is also interested in the study of chaperones. He was awarded a National Natural Science Prize, First Class in 1981 and again in 1987. He was awarded the Prize in Life Sciences of the Third World Academy of Sciences in 1993 for his contribution to enzyme inhibition kinetics. He has won the National Natural Science Award first class twice, and second class four times.
His autobiography has appeared in Comprehensive Biochemistry Vol. 37 as part of the History of Biochemistry.