Influences of the Hydrophobicity of the Heme-binding Pocket on the Propreties and Functions of Cytochrome b5 Mutants

• 来源期刊: 中国化学（英文版）
• 年，卷（期）: 2003,（10）
• 页码范围: 1385-1389
• 页数: 5页
• 语种: 英文

摘要

The mutation sites of the four mutants F35Y, P40V, V45E and V45Y of cytochrome b5 are located at the edge of the hemebinding pocket. The solvent accessible areas of the "pocket interior" of the four mutants and the wild-type cytochrome b5 have been calculated based on their crystal structures at high resolution. The change in the hydrophobicity of the heme-binding pocket resulting from the mutation can be quantitatively described using the difference of the solvent accessible area of the "pocket interior" of each mutant from that of the wild-type cytochrome b5. The influences of the hydrophobicity of the hemebinding pocket on the protein stability and redox potential are discussed.