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《Acta Chimica Sinica》 2003-01
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Effect of Pb~(2+) on RNase Activity and Its Structure

HONG, Fa-Shui ,a WANG, Ling b WU, Kang a WANG, Xue-Feng a ( a College of Life Sciences, bLibrary, Suzhou University, Suzhou 215006) TAO, Ye (Synchrotron Radiation Laboratory, Institute of High Energy Physics, The Chinese Academy of Sciences, Beijing 100039)  
Activity of RNase from porcine pancreas was enhanced by treatment with Pb 2+ at low concentration (0.17×10 -2~0.6×10 -2 μmol/L) but was inhibited by Pb 2+ at high concentration (over 0.85×10 -2 μmol/L ). Pb 2+ at high concentration could competitively displace Ca 2+ from RNase and the fluorescence titration showed that one molecule of RNase had three binding sites for Pb 2+, the association constant k_ sv for its low-affinity Pb 2+-binding site was 6.03×10 6 (mol/L) -1. The extended X-ray absorption fine structure (EXAFS) spectrum demonstrated that Pb 2+ coordinated nitrogen or oxygen atoms of the active site of RNase or other amino acid residue of RNase, Pb-N (or O) bond length was 0.242 nm and 0.312 nm, and coordination number was 2, respectively. The secondary structure of RNase was greatly damaged by Pb 2+ at high concentration resulting in the decrease of α-helix, β-sheet and β-turn contents and the increase of random coil contents.
【Fund】: 苏州大学人才引进基金(No.XQ31 60 1 1 )资助项目
【CateGory Index】: O657.3
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