Thomas_Bruice

Thomas Bruice

Thomas Bruice

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Thomas C. Bruice (August 25, 1925 – February 15, 2019)[1] was a professor of chemistry and biochemistry at University of California, Santa Barbara. He was elected to the National Academy of Sciences in 1974. He was a pioneering researcher in the area of chemical biology, and is one of the 50 most cited chemists.[2][3]

Quick Facts Born, Died ...

Education

Bruice earned his B.S. at the University of Southern California, and returned there after his service as a Marine medical corpsman during the World War II island campaigns in the South Pacific, and obtained his Ph.D. there.[1] He carried out post-doctoral work at University of California, Los Angeles. He has been a faculty member at Yale University, Johns Hopkins University, and Cornell University.[2] He joined the faculty at the University of California, Santa Barbara in 1964.

Research

Papers

Bruice published more than 600 papers during his career. He saw himself as a bioorganic chemist rather than as a biochemist, and that description is very apt for his work, as most of the molecules that he studied were natural products such as thyroxine.[4] In addition, he made important contributions to understanding enzyme catalysis, and he pioneered the use of imidazole-catalysed hydrolysis of p-nitrophenyl acetate as a model system.[5] (This system has the practical advantage that it is very convenient to follow the hydrolysis spectrophotometically.) He also stied[check spelling] a similar reaction catalysed by the enzyme ribonuclease.[6] More generally, he made a study of mechanisms for chymotrypsin catalysis.,[7] and in particular the "charge-relay" system as a way of understanding the role of the catalytic triad that exists in such enzymes.[8] He considered that "orbital steering" was a new name for a well established observation.[9][10]

Reviews

Bruice wrote reviews on a number of topics, including the use of small molecules to understand catalysis [11] and the chemistry of flavins,[12][13] and on enzyme catalysis in general.[14]

Books

Bruice collaborated with Stephen Benkovic to write a two-volume work on Bioorganic Mechanisms that helped establish this field.[15]

Awards and honors

References

  1. [1]
    Benkovic, Stephen J. (2019). "Thomas Bruice (1925–2019)". Proceedings of the National Academy of Sciences. 116 (45): 22418–22419. Bibcode:2019PNAS..11622418B. doi:10.1073/pnas.1913522116. PMC 6842622. PMID 31636196.
  2. [2]
    "2008 Pauling Award Symposium". The University of British Columbia. 2008. Archived from the original on 4 February 2011. Retrieved 6 January 2011.
  3. [3]
    "Dr. Thomas C. Bruice, Bio-Organic Chemistry Pioneer". The LACC Foundation. Archived from the original on 16 December 2010. Retrieved 6 January 2011.
  4. [4]
    Bruice, Thomas C.; Kharasch, Norman; Winzler, Richard J. (1956). "A correlation of thyroxine-like activity and chemical structure". Archives of Biochemistry and Biophysics. 62 (2): 305–317. doi:10.1016/0003-9861(56)90129-1. PMID 13328119.
  5. [5]
    Bruice, Thomas C.; Schmir, Gaston L. (1956). "The catalysis of the hydrolysis of p-nitrophenyl acetate by imidazole and its derivatives". Archives of Biochemistry and Biophysics. 63 (2): 484–486. doi:10.1016/0003-9861(56)90068-6. PMID 13355478.
  6. [6]
    Bruice, Thomas C.; Holmquist, Barton.; Stein, Thomas Peter. (1967). "Reaction of ribonuclease a with o-nitrophenyl hydrogen oxalate". Journal of the American Chemical Society. 89 (16): 4221–4222. doi:10.1021/ja00992a047. PMID 6045612.
  7. [7]
    Bruice, T. C. (1961). "The Mechanisms for Chymotrypsin". Proceedings of the National Academy of Sciences. 47 (12): 1924–1928. Bibcode:1961PNAS...47.1924B. doi:10.1073/pnas.47.12.1924. PMC 223243. PMID 13873928.
  8. [8]
    Rogers, Gary A.; Bruice, Thomas C. (1974). "Synthesis and evaluation of a model for the so-called charge-relay system of the serine esterases". Journal of the American Chemical Society. 96 (8): 2473–2481. doi:10.1021/ja00815a028. PMID 4833707.
  9. [9]
    Bruice, T. C.; Pandit, U. K. (1960). "Intramolecular Models Depicting the Kinetic Importance of "Fit" in Enzymatic Catalysis". Proceedings of the National Academy of Sciences. 46 (4): 402–404. Bibcode:1960PNAS...46..402B. doi:10.1073/pnas.46.4.402. PMC 222851. PMID 16590620.
  10. [10]
    Bruice, T. C.; Brown, A.; Harris, D. O. (1971). "On the Concept of Orbital Steering in Catalytic Reactions". Proceedings of the National Academy of Sciences. 68 (3): 658–661. Bibcode:1971PNAS...68..658B. doi:10.1073/pnas.68.3.658. PMC 389011. PMID 16591915.
  11. [11]
    Bruice, T. C. (1976). "Some Pertinent Aspects of Mechanism as Determined with Small Molecules". Annual Review of Biochemistry. 45: 331–374. doi:10.1146/annurev.bi.45.070176.001555. PMID 786153.
  12. [12]
    Bruice, Thomas C. (1980). "Mechanisms of flavin catalysis". Accounts of Chemical Research. 13 (8): 256–262. doi:10.1021/ar50152a002.
  13. [13]
    Bruice, T.C. (1984). "Oxygen-flavin chemistry". Israel Journal of Chemistry. 24 (1): 54–61. doi:10.1002/ijch.198400008.
  14. [14]
    Bruice, Thomas C.; Benkovic, Stephen J. (2000). "Chemical Basis for Enzyme Catalysis". Biochemistry. 39 (21): 6267–6274. doi:10.1021/bi0003689. PMID 10828939.
  15. [15]
    Bruice, T.C.; Benkovic, S.J. (1966). Bioorganic Mechanisms. New York: Benjamin, Inc.
  16. [16]
    "Linus Pauling Medalists". Portland State University. Retrieved 7 January 2011.
  17. [17]
    "About the NAS Award in Chemical Sciences". National Academy of Sciences. Retrieved 5 June 2017.
  18. [18]
    "Academy Honors 17 for Major Contributions to Science". The National Academy of Sciences. 26 January 2005. Retrieved 7 January 2011.
  19. [19]
    "SCALACS Tolman Awards". American Chemical Society. Retrieved 23 April 2014.
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