De Novo design and utilization of photolabile caged substrates as probes of hydrogen tunneling with horse liver alcohol dehydrogenase at sub-zero temperatures: a …

SC Tsai, JP Klinman

Index: Tsai, Shiou-Chuan; Klinman, Judith P. Bioorganic Chemistry, 2003 , vol. 31, # 2 p. 172 - 190

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Citation Number: 28

Abstract

In order to understand the influence of protein dynamics on enzyme catalysis and hydrogen tunneling, the horse liver alcohol dehydrogenase (HLADH) catalyzed oxidation of benzyl alcohol was studied at sub-zero temperatures. Previous work showed that wild type HLADH has significant kinetic complexity down to− 50° C due to slow binding and loss of substrate [S.-C. Tsai, JP Klinman, Biochemistry, 40 (2001) 2303]. A strategy was therefore ...