|Table of Contents|

Interaction of LSPcZn and Myoglobin(PDF)

《南京师范大学学报》(自然科学版)[ISSN:1001-4616/CN:32-1239/N]

Issue:
2016年02期
Page:
28-
Research Field:
化学
Publishing date:

Info

Title:
Interaction of LSPcZn and Myoglobin
Author(s):
Wang YueWang AoZhou LinWei Shaohua
School of Chemistry and Materials Science,Nanjing Normal University,Nanjing 210023,China
Keywords:
PhthalocyanineFePP-Mbinteractionfluorescence spectroscopy
PACS:
O657.39
DOI:
10.3969/j.issn.1001-4616.2016.02.006
Abstract:
The interaction of LSPcZn and myoglobin was studied under the physiological condition. The LSPcZn can quench the fluorescence of those three kinds of proteins’ myoglobin effectively,and it is indicated that there is a strong interaction occurring between LSPcZn and myoglobin. The results of the fluorescence spectra with changing temperature proved that the interaction can lead to the formation of complex of LSPcZn with myoglobin,and quench the fluorescence of myoglobin through the static quenching mechanism. Dealing with the values of fluorescence spectra,we obtained the binding constant and binding site of complexs between LSPcZn and myoglobin under different tempeture. In addition,the interaction can change the conformation of myoglobin markedly also.

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Last Update: 2016-06-30