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个人信息Personal Information
教授
博士生导师
硕士生导师
主要任职：中国化学会创始会士、常务理事，中国化工学会会士
性别：男
毕业院校：大连理工大学
学位：博士
所在单位：化工学院
学科：应用化学. 精细化工. 化学生物学
办公地点：大连理工大学西部校区知顺楼F-202#
http://peng-group.dlut.edu.cn/
联系方式：大连理工大学西部校区知顺楼F-202 辽宁省大连市高新区凌工路2号，大连116024 课题组网址：http://peng-group.dlut.edu.cn/ E-mail: pengxj@dlut.edu.cn
电子邮箱：pengxj@dlut.edu.cn
Site-Directed Mutagenesis of Myoglobin for Studies of Their Interaction with Iron(III) by Multi-Spectroscopic Techniques
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论文类型：期刊论文
发表时间：2013-01-01
发表刊物：JOURNAL OF SPECTROSCOPY
收录刊物：SCIE、EI、Scopus
卷号：1
期号：1
ISSN号：2314-4920
摘要：In order to investigate how the amino acids on the surface of myoglobin molecule influence myoglobin's structure and function, a variety of spectroscopy techniques were applied in the study of the interaction between Fe(III) and myoglobin (wild type and its mutants, D44K, D60K, and K56D). The results demonstrated that(III) can quench the flourescence of wild type and mutants of myoglobin, and quenching mechanisms are static quenching. it is found that the biding distance between Fe(III) and myoglobin mutants gets smaller, the binding capacity increases by the values of binding constant and the bimolecular quenching constant as well as the binding distance. Those data also indicate that the metal ion Fe(III) can interact strongly with myoglobin mutants. The three-dimensional conformation change after surface amino acids are replaced is detected by the UV absorption spectroscopy and flourescence spectroscopy, which make mutants become more dynamic and change its function and interaction with Fe(III) strongly.