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Marion Hugh O'Leary

Affiliations: 
1967-1989 Chemistry University of Wisconsin, Madison, Madison, WI 
Website:
https://prabook.com/web/marion_hugh.o_leary/818019
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"Marion Hugh O'Leary"
Bio:

https://www.gf.org/fellows/all-fellows/marion-h-oleary/
DOI: 10.1021/ar00156a003
Marion H. O’Leary was born in Quincy, IL, in 1941. He received his undergraduate degree at the University of Illinois, where he worked under S. G. Smith, and his Ph.D. at M.I.T., where he worked under C . G. Swain. In 1966-1967 he was a postdoctoral fellow in the laboratory of F. H. Westheimer at Harvard. Since 1967 he has been at the University of Wisconsin-Madison. His research interests are in the application of stable isotopes to problems in biochemistry and biology and in the mechanisms of enzymatic reactions

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Parents

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Stanley Glen Smith research assistant 1963 UIUC
C. Gardner Swain grad student 1966 MIT
 (Studies of oxygen and chlorine isotope effects and oxygen exchange in the hydrolysis of benzoyl chloride.)
Frank H. Westheimer post-doc 1966-1967 Harvard

Children

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John William Keller post-doc 1976-1979 UW Madison

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Publications

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Robinson JJ, Scott KM, Swanson ST, et al. (2003) Kinetic isotope effect and characterization of form II RubisCO from the chemoautotrophic endosymbionts of the hydrothermal vent tubeworm Riftia pachyptila Limnology and Oceanography. 48: 48-54
Swanson T, Brooks HB, Osterman AL, et al. (1998) Carbon-13 isotope effect studies of Trypanosoma brucei ornithine decarboxylase. Biochemistry. 37: 14943-7
Pawlak J, O'Leary MH, Paneth P. (1998) Are mutated enzymes good models for interpretation of intrinsic isotope effects Journal of Molecular Structure-Theochem. 454: 69-75
Sun S, Smith GS, O'Leary MH, et al. (1997) The linkage of catalysis and regulation in enzyme action. Fluoropyruvate as a probe of regulation in pyruvate decarboxylases Journal of the American Chemical Society. 119: 1507-1515
Stoker PW, O'Leary MH, Boehlein SK, et al. (1996) Probing the mechanism of nitrogen transfer in Escherichia coli asparagine synthetase by using heavy atom isotope effects. Biochemistry. 35: 3024-30
Madhavan S, Andreo CS, Maurino VG, et al. (1996) In Situ Localization of Nadp-Malic Enzyme in Bundle Sheath Cells and Leaf Carbon Isotope Fractionation in Two C4 Grasses International Journal of Plant Sciences. 157: 118-122
Szylhabel‐Godala A, Madhavan S, Rudziński J, et al. (1996) Nitrogen and deuterium kinetic isotope effects on the Menshutkin reaction Journal of Physical Organic Chemistry. 9: 35-40
Gawlita E, Caldwell WS, O'Leary MH, et al. (1995) Kinetic isotope effects on substrate association: Reactions of phosphoenolpyruvate with phosphoenolpyruvate carboxylase and pyruvate kinase Biochemistry. 34: 2577-2583
Bong Ho Lee, Ley BW, Kantrowitz ER, et al. (1995) Domain closure in the catalytic chains of Escherichia coli aspartate transcarbamoylase influences the kinetic mechanism Journal of Biological Chemistry. 270: 15620-15627
Wedler FC, Ley BW, Lee BH, et al. (1995) L-aspartate association contributes to rate limitation and induction of the T → R transition in Escherichia coli aspartate transcarbamoylase: Equilibrium exchanges and kinetic isotope effects with a Vmax-enhanced mutant, Asp-236 → Ala Journal of Biological Chemistry. 270: 9725-9733
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