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《Chemical Research In Chinese Universities》 2002-01
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Resonance Raman Spectroscopic Study of Cytochrome c Mutants

ZHENG Jun Wei *, GU Ren Ao (Department of Chemistry, Suzhou University, Suzhou 215006, China) LU Tian Hong (Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, Changchun 130022, China)  
The spectroscopic characteristics of cytochrome c(WT) and its mutants(Y67F and N52I) in the low frequency region were studied by Resonance Raman technique. The results show that the replacement of phenylalanine for Tyr 67 in WT had a very slight effect on the hydrogen bonding and conformation of the amino acid residues around propionic acid side chains of heme group. However, large effects on the hydrogen bonding of internal water with its surrounding amino acid residues and hydrophobility of the heme cavity were observed as Asn 52 was substituted with isoleucine, which resulted in conformational regulations of heme group and surrounding amino acid residues.
【Fund】: 国家自然科学基金 (批准号 :2 0 0 730 2 8);; 苏州大学启动基金资助
【CateGory Index】: O657.37
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