William Wallace Cleland | |
|---|---|
 | |
| Born | (1930-01-06)January 6, 1930 |
| Died | March 6, 2013(2013-03-06) (aged 83) |
| Alma mater | Oberlin College(A.B., 1950) University of Wisconsin(M.S., 1953) (Ph.D., 1955) |
| Known for | Enzyme kinetics and mechanism |
| Awards | Repligen Award |
| Scientific career | |
| Fields | Biochemistry |
| Institutions | University of Wisconsin |
William Wallace Cleland (January 6, 1930 – March 6, 2013[1], often cited asW. W. Cleland, and known almost universally as "Mo Cleland", was aUniversity of Wisconsin-Madison biochemistry professor. His research was concerned withenzyme reaction mechanism andenzyme kinetics,[2] especially multiple-substrate enzymes. He was elected to theNational Academy of Sciences in 1985.
Cleland was born in 1930 inBaltimore, Maryland. He received his A.B. fromOberlin College in 1950 and his M.S. and Ph.D. from the University of Wisconsin–Madison in 1953 and 1955, respectively.[3] He was an avid stamp collector and was awarded the Lifetime Achievement Award inPhilately by theSmithsonian Institution in 2008. Cleland died on March 6, 2013, after falling on ice.[4]
After carrying out postdoctoral research at theUniversity of Chicago he returned to University of Wisconsin–Madison, where he became assistant professor in 1959. In 1962 he was promoted to associate professor and then professor in 1966. He became J. Johnson Professor of Biochemistry in 1978, and Steenbock Professor of Chemical Science in 1982.[2]
Kresge, Simoni and Hill[5] have presented a general appreciation of Cleland's life and career.
Cleland's research focused on the use ofenzyme kinetics to deduce enzyme mechanisms, especially those involved in phospho and acyl transfers.[3] He pioneered the kinetic and mechanistic study of enzymes with more than one substrate, and he was probably the first to make a systematic classification of mechanisms and the corresponding kinetic equations.[6][7][8] Building on this work he made kinetic studies of various enzymes, including isotope exchange of creatine kinase.[9]
Cleland was a pioneer in the use of computers to analyze enzyme kinetic data,[10] and hisFortran programs that implement Wilkinson's analysis,[11] which he distributed to anyone who requested them, were very influential.
In the latter part of his career Cleland contributed greatly to studies of the use of kinetic isotope effects as a tool for elucidating mechanisms of enzyme catalysis.[12]
He was the first to usedithiothreitol for the reduction of disulfide bonds in proteins, and the compound is accordingly often called Cleland's reagent.[13]
Enzyme Kinetics and Mechanism (with P. F. Cook, 2007)[14]
