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Journal of Spectroscopy
30217 Vol.2013, 000(2013)
p.11-11
Site-Directed Mutagenesis of Myoglobin for Studies of Their Interaction with Iron(III) by Multi-Spectroscopic Techniques
Qian Tang[1,2]; Xiao-Jun Peng[1]; Hong-Yu Cao[2]; Yan-Jie Yang[2]; Jing Ma[2]; Jing-Yun Wang[1]; and Xue-Fang Zheng[2];
[1]Faculty of Environmental and Biological Science and Technology, Dalian University of Technology, Dalian City 116024, China [2]Liaoning Key Laboratory of Bioorganic Chemistry, Dalian University, Dalian City 116622, China
 Abstract: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 demonstrate that Fe(III) can quench the fluorescence of wild type and mutants of myoglobin, and the quenching mechanisms are static quenching. It is found that the binding 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 fluorescence spectroscopy, which make mutants become more dynamic and change its function and interaction with Fe(III) strongly.
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