Spectroscopy and Spectral Analysis, Volume. 31, Issue 9, 2512(2011)
Comparison between Myoglobin and Its Mutant(D60K) Interacting with Hydrogen Peroxide by Spectrum
To characterize the roles played by surface-charged residue Asp60 in the structure stability of myoglobin when it was replaced with Lys, the interaction of myoglobin[Mb(WT)] and its mutant[Mb(D60K)] with hydrogen peroxide (H2O2) were studied by the method of ultraviolet-visible (UV-Vis) absorption spectroscopy, fluorescence spectroscopy and stopped-flow fluorescence spectroscopy under simulative physiological conditions. There are remarkable differences between Mb(D60K) and Mb(WT) in the UV-Vis absorption spectroscopy and fluorescence spectroscopy of iron porphyrin during the process of interaction. Although we only altered one external amino acide, the data showed that the function and structure stability of Mb(D60K) was greatly changed. Furthermore, results from synchronous fluorescence spectroscopy and stopped-flow fluorescence spectroscopy all indicated that H2O2 had less effect on the structure of Mb(D60K) while the structure of Mb(WT) was notably changed. From a comprehensive and comparative data analysis, the authors determined that the structure of Mb(D60K) was improved when it interacted with H2O2.
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ZHI Qiu-yan, TANG Qian, CAO Hong-yu, AN Liang-mei, ZHANG Ying-ying, ZHENG Xue-fang. Comparison between Myoglobin and Its Mutant(D60K) Interacting with Hydrogen Peroxide by Spectrum[J]. Spectroscopy and Spectral Analysis, 2011, 31(9): 2512
Received: Nov. 30, 2010
Accepted: --
Published Online: Nov. 9, 2011
The Author Email: Qiu-yan ZHI (dlzhiqy@163.com)