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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.