Role of internal thermodynamics in determining hydrogen tunneling in enzyme-catalyzed hydrogen transfer reactions.
Previous investigations have indicated a role for hydrogen tunneling in the yeast alcohol dehydrogenase catalyzed oxidation of benzyl alcohol [Cha, Y., Murray, C. J., & Klinman, J. P. (1989) Science 243, 1325] and the bovine plasma amine oxidase catalyzed oxidation of benzylamine [Grant, K.L., & Klinman, J. P. (1989) Biochemistry 28,6597]. In the present studies, values of protium to tritium and deuterium to tritium isotope effects and their temperature dependencies have been measured using ring-substituted substrates for yeast alcohol dehydrogenase and bovine plasma amine oxidase, revealing tunneling in each case. The results of these studies indicate that hydrogen tunneling is a general phenomenon and is not limited to enzyme reactions with degenerate energy levels for bound substrates and products. An analysis of internal thermodynamics in the yeast alcohol dehydrogenase reaction shows that tunneling occurs when delta H degrees is endothermic and that the degree of tunneling appears to increase as delta H degrees decreases toward zero.
Rucker
J
J
Department of Chemistry, University of California, Berkeley 94720.
Cha
Y
Y
Jonsson
T
T
Grant
K L
KL
Klinman
J P
JP
D000426:Alcohol Dehydrogenase / Q000378:metabolism*; D006631:Amine Oxidase (Copper-Containing); D000818:Animals; D001592:Benzyl Alcohols / Q000737:chemistry; D002384:Catalysis; D002417:Cattle; D006859:Hydrogen / Q000737:chemistry*; D010084:Oxidation-Reduction; D000587:Oxidoreductases Acting on CH-NH Group Donors / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D013816:Thermodynamics
D001592:Benzyl Alcohols; D006859:Hydrogen; D000426:Alcohol Dehydrogenase; D006631:Amine Oxidase (Copper-Containing); D000587:Oxidoreductases Acting on CH-NH Group Donors