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Converting Cytochrome b 5 into Cytochrome c‐Like Protein
Author(s) -
Lin YingWu,
Wang WenHu,
Zhang Qi,
Lu HaoJie,
Yang PengYuan,
Xie Yi,
Huang ZhongXian,
Wu HouMing
Publication year - 2005
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200500030
Subject(s) - hemeprotein , heme , cytochrome , chemistry , cytochrome c , covalent bond , cytochrome b5 , function (biology) , computational biology , reactivity (psychology) , protein–protein interaction , biochemistry , stereochemistry , computer science , biology , genetics , enzyme , organic chemistry , mitochondrion , medicine , alternative medicine , pathology
Covalent attachment of a heme group to a protein matrix (see picture) allows a direct comparison of the properties of proteins in the same protein scaffold to be made. Using cytochrome b 5 as the model will enable us to elucidate the precise role of the heme–protein covalent interaction that governs functional diversity and to delineate the “structure–property–reactivity–function” relationship of hemoproteins.