Impact of Protein Flexibility on Hydride-Transfer ... - ACS Publications

Impact of Protein Flexibility on Hydride-Transfer Parameters in Thermophilic and Psychrophilic Alcohol Dehydrogenases [J. Am. Chem. Soc. 2004, 126 ...
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Impact of Protein Flexibility on Hydride-Transfer Parameters in Thermophilic and Psychrophilic Alcohol Dehydrogenases [J. Am. Chem. Soc. 2004, 126, 95009501]. Zhao-Xun Liang, Iason Tsigos, Vassilis Bouriotis, and Judith P. Klinman* We have now determined that the mutant designated P86A in this paper is, in actuality, P56A. We attribute this error to a visual mistracking along the DNA sequence, such that primers were constructed to alter the proline at position 56. P56 lies on a surface-exposed loop in the substrate-binding domain, ca. 18 Å away from the bound trifluoroethanol; the corresponding position is either deleted or a proline in the mesophilic and psychrophilic alcohol dehydrogenases, respectively. A comparison of the properties of P86A and P56A will be published at a later date. JA069955T 10.1021/ja069955t Published on Web 02/17/2006

An Annulation toward Fused Bicyclolactones [J. Am. Chem. Soc. 2005, 127, 17184-17185]. Rene-Viet Nguyen and Chao-Jun Li* Page 17185, Table 2. The structure 3a-j in the equation was mistakenly drawn as trans-fused. The two rings in the structure should be cis-fused. We apologize for this error. JA060508N 10.1021/ja060508n Published on Web 02/21/2006