caa a22 4500 475743997 CHVBK 20180406123507.0 cr unu---uuuuu 170329e20000801xx s 000 0 eng 10.1023/A:1026597314542 doi (NATIONALLICENCE)springer-10.1023/A:1026597314542 Effects of Ca2+ on the Activity and Stability of Methanol Dehydrogenase [Elektronische Daten] [Yongfang Zhao, Guanfang Wang, Zhifang Cao, Yinshan Wang, Hui Cheng, Hai-Meng Zhou] The effects of exogenously added Ca2+ on the enzymatic activity and structural stability of methanol dehydrogenase were studied for various Ca2+ concentrations. Methanol dehydrogenase activity increased significantly with increasing concentration of Ca2+, approaching saturation at 200 mM Ca2+. The effect of Ca2+ on the activation of MDH was time dependent and Ca2+ specific and was due to binding of the metal ions to the enzyme. Addition of increasing concentration of Ca2+ caused a decrease of the intrinsic tryptophan fluorescence intensity in a concentration-dependent manner to a minimum at 200 mM, but with no change in the fluorescence emission maximum wavelength or the CD spectra. The results revealed that the activation of methanol dehydrogenase by Ca2+ occurred concurrently with the conformational change. In addition, exogenously bound Ca2+ destabilized MDH. The potential biological significance of these results is discussed. Plenum Publishing Corporation, 2000 Methanol dehydrogenase nationallicence Ca2+ nationallicence binding nationallicence activity nationallicence stability nationallicence Zhao Yongfang Department of Biochemistry and Biophysics, College of Life Sciences, Wuhan University, 430072, Wuhan, China aut Wang Guanfang Department of Biochemistry and Biophysics, College of Life Sciences, Wuhan University, 430072, Wuhan, China aut Cao Zhifang Department of Biological Sciences and Biotechnology, Tsinghua University, 100084, Beijing, China aut Wang Yinshan Wuhan Institute of Virology, Academia Sinica, 430071, Wuhan, China aut Cheng Hui Wuhan Institute of Virology, Academia Sinica, 430071, Wuhan, China aut Zhou Hai-Meng Department of Biological Sciences and Biotechnology, Tsinghua University, 100084, Beijing, China aut Journal of Protein Chemistry Kluwer Academic Publishers-Plenum Publishers 19/6(2000-08-01), 469-473 0277-8033 19:6<469 2000 19 10930 https://doi.org/10.1023/A:1026597314542 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1023/A:1026597314542 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Zhao Yongfang Department of Biochemistry and Biophysics, College of Life Sciences, Wuhan University, 430072, Wuhan, China aut NATIONALLICENCE 700 1- Wang Guanfang Department of Biochemistry and Biophysics, College of Life Sciences, Wuhan University, 430072, Wuhan, China aut NATIONALLICENCE 700 1- Cao Zhifang Department of Biological Sciences and Biotechnology, Tsinghua University, 100084, Beijing, China aut NATIONALLICENCE 700 1- Wang Yinshan Wuhan Institute of Virology, Academia Sinica, 430071, Wuhan, China aut NATIONALLICENCE 700 1- Cheng Hui Wuhan Institute of Virology, Academia Sinica, 430071, Wuhan, China aut NATIONALLICENCE 700 1- Zhou Hai-Meng Department of Biological Sciences and Biotechnology, Tsinghua University, 100084, Beijing, China aut NATIONALLICENCE 773 0- Journal of Protein Chemistry Kluwer Academic Publishers-Plenum Publishers 19/6(2000-08-01), 469-473 0277-8033 19:6<469 2000 19 10930 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer