William Wallace Cleland
Born(1930-01-06)January 6, 1930
Baltimore, Maryland
DiedMarch 6, 2013(2013-03-06) (aged 83)
Alma materOberlin College (A.B., 1950)
University of Wisconsin (M.S., 1953) (Ph.D., 1955)
Known forEnzyme kinetics and mechanism
AwardsRepligen Award
Scientific career
FieldsBiochemistry
InstitutionsUniversity of Wisconsin

William Wallace Cleland (January 6, 1930 – March 6, 2013[1], often cited as W. W. Cleland, and known almost universally as "Mo Cleland", was a University of Wisconsin-Madison biochemistry professor. His research was concerned with enzyme reaction mechanism and enzyme kinetics,[2] especially multiple-substrate enzymes. He was elected to the National Academy of Sciences in 1985.

Life and education

Cleland was born in 1930 in Baltimore, Maryland. He received his A.B. from Oberlin 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 in Philately by the Smithsonian Institution in 2008. Cleland died on March 6, 2013, after falling on ice.[4]

Career

After carrying out postdoctoral research at the University 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.

Scientific contributions

Papers

Cleland's research focused on the use of enzyme 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 his Fortran 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 use dithiothreitol for the reduction of disulfide bonds in proteins, and the compound is accordingly often called Cleland's reagent.[13]

Book

Enzyme Kinetics and Mechanism (with P. F. Cook, 2007)[14]

Awards and recognition

References

  1. ^ "In Memoriam". National Academy of Sciences. Retrieved 8 March 2013.
  2. ^ a b Academic home page
  3. ^ a b c d e f g J. Biol. Chem. biographical article
  4. ^ "Biochemistry Mourns the Loss of "Mo" Cleland". News 2013. Department of Biochemistry, UW-Madison. 6 March 2013. Retrieved 9 March 2013.
  5. ^ Kresge; Simoni, Robert D.; Hill, Robert L. (2006). "Determining enzyme mechanisms by kinetic analysis: The work of W. Wallace Cleland". J. Biol. Chem. 281 (46): e37. doi:10.1016/S0021-9258(19)35036-7.
  6. ^ Cleland, W.W (1963). "The kinetics of enzyme-catalyzed reactions with two or more substrates or products". Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects. 67: 188–196. doi:10.1016/0926-6569(63)90227-X.
  7. ^ Cleland, W.W (1963). "The kinetics of enzyme-catalyzed reactions with two or more substrates or products". Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects. 67: 104–137. doi:10.1016/0926-6569(63)90211-6.
  8. ^ Cleland, W.W (1963). "The kinetics of enzyme-catalyzed reactions with two or more substrates or products". Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects. 67: 173–187. doi:10.1016/0926-6569(63)90226-8.
  9. ^ Morrison, J.F.; Cleland, W.W. (1966). "Isotope Exchange Studies of the Reaction Catalyzed by Adenosine Triphosphate: Creatine Phosphotransferase". J. Biol. Chem. 241 (3): 673–683. doi:10.1016/S0021-9258(18)96891-2.
  10. ^ Cleland, W. W. (1963). "Computer Programmes for Processing Enzyme Kinetic Data". Nature. 198 (4879): 463–465. Bibcode:1963Natur.198..463C. doi:10.1038/198463a0. PMID 14021666. S2CID 4261285.
  11. ^ Wilkinson, GN (1961). "Statistical estimations in enzyme kinetics". Biochemical Journal. 80 (2): 324–332. doi:10.1042/bj0800324. PMC 1244002. PMID 13785321.
  12. ^ Cleland, W. W. (2007). "Use of isotope effects to determine enzyme mechanisms". Journal of Labelled Compounds and Radiopharmaceuticals. 50 (11–12): 1006–1015. doi:10.1002/jlcr.1390.
  13. ^ Cleland, W.W. (April 1964). "Dithiothreitol, A New Protective Reagent for SH Groups". Biochemistry. 3 (4): 480–2. doi:10.1021/bi00892a002. PMID 14192894.
  14. ^ Cook, Paul; Cleland, William Wallace (2007). Enzyme kinetics and mechanism. London: Garland Science. ISBN 978-0-8153-4140-6.
  15. ^ "Cleland, W. Wallace "Mo"". Madison.com. March 10, 2013. Retrieved 12 March 2013.
  16. ^ "36th Symposium: Enzyme Structure and Function". University of Wisconsin–Madison. Retrieved 29 August 2023.

External links

Repligen Corporation Award in Chemistry of Biological Processes
Authority control databases
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