Article
X-ray crystallography, CD and kinetic studies revealed the essence of the abnormal behaviors of the cytochrome b5 Phe35-->Tyr mutant.
European journal of biochemistry - 1 Sept 2002
Yao Ping, Wu Jian, Wang Yun-Hua, Sun Bing-Yun, Xia Zong-Xiang, Huang Zhong-Xian
Abstract excerpt
Conserved phenylalanine 35 is one of the hydrophobic patch residues on the surface of cytochrome b5 (cyt b5). This patch is partially exposed on the surface of cyt b5 while its buried face is in direct van der Waals' contact with heme b. Residues Phe35 and Phe/Tyr74 also form an aromatic channel with His39, which is one of the axial ligands of heme b. By site-directed mutagenesis we have produced three mutants of...
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