NDLI: Study on the DME-cytochromeb $_{5}$ and its mutants at site of F58

Content Provider	Springer Nature Link
Author	Su, Hui Lu, Junxia Wang, Yunhua Ren, Yi Xie, Yi Huang, Zhongxian
Copyright Year	2004
Abstract	Phenylalanine-58 is one of the conservative residues in the hydrophobic pocket of Cytb $_{5}$, which forms aromatic stacking with the hemeb. Previous study showed that both the stacking and the property of the aromatic residue affect hydrophobicity of the heme pocket, leading to change of protein’s property. In order to further reveal the essence we esterify the heme propionate of Cytb $_{5}$, F58Y.and F58W, and eliminate the hydrogen bond between heme propionate and Ser64 in examining the effect of hydrogen net on the π-π interaction. In this paper thermal denaturation of DME-Cytb $_{5}$ and its F58Y.and F58W mutants has been studied by UV-visible and CD spectra. The heme transfer reactions between these proteins and apo-myoglobin have been studied as well. The results demonstrate that esterification did not destroy the aromatic stacking; however, it affects the stability of the proteins due to different volumes, hydrophobicities and hydrogen bonds forming ability of these substituents.
Starting Page	1914
Ending Page	1919
Page Count	6
File Format	PDF
ISSN	10016538
Journal	Chinese Science Bulletin
Volume Number	49
Issue Number	18
e-ISSN	18619541
Language	English
Publisher	Science in China Press
Publisher Date	2004-01-01
Publisher Place	Beijing
Access Restriction	Subscribed
Subject Keyword	Cytb $_{5}$ aromatic stacking effect esterified heme Science Life Sciences Physics Chemistry/Food Science Earth Sciences Engineering
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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