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Comparison of inactivation and conformational changes of native and apo yeast alcohol dehydrogenase during thermal denaturation
Author(s) -
Yang Yi,
Chen Rong,
Zhou HaiMeng
Publication year - 1998
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549800202862
Subject(s) - chemistry , denaturation (fissile materials) , alcohol dehydrogenase , circular dichroism , conformational change , enzyme , zinc , yeast , fluorescence , native state , biophysics , crystallography , biochemistry , stereochemistry , organic chemistry , nuclear chemistry , physics , quantum mechanics , biology
Abstract The conformational changes of native and apo yeast alcohol dehydrogenase during thermal denaturation have been followed by fluorescence emission and circular dichroism spectra. A comparison of inactivation and conformational changes during thermal denaturation shows that for the native enzyme and for the apo‐I YADH which has the conformational zinc removed, the extent of inactivation was larger than the extent of conformational changes at the same temperature. This result supported the suggestion by Tsou (Trends Biochem. Sci. 1986, 11, 427‐429: Science 1993, 262, 380‐381) that the enzyme active site is more flexible. The results also show that apo‐I YADH without the conformational zinc was more easily inactivated with increasing incubation temperature, indicating that the stability of the apo‐I YADH decreased. Kinetic analysis suggest that the substrate does not provide any protective effect during thermal inactivation of native and apo‐I YADH.