期刊论文

Lin, Ying-Wu

英文

SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY

1386-1425

2012

96

365-369

10.1016/j.saa.2012.05.065

To test the possibility of heme transfer from a heme protein to a heme-binding DNA aptamer, we chose microsomal bovine cyt b5 and heme–aptamer, PS2.M, as an example, respectively, and performed heme transfer experiment. As shown in Fig. 2A, ferric WT cyt b5 exhibits a characteristic Soret band at 413 nm in UV–visible spectrum. Upon WT cyt b5 exposure to 2 equivalents of PS2.M, the Soret band decreased with time and a shoulder peak appeared around 404 nm, characteristic of a PS2.M–heme complex,

本校为第一且通讯机构

Heme transfer is commonly observed from one heme protein to the other such as from cytochrome b5 (cyt b5) to apo-myoglobin. In this study, instead of to another heme protein, we observed the heme transfer from wild-type (WT) cyt b5, H39C cyt b5 with heme axial ligand His39 mutated to Cys39, and DME cyt b5 with heme replaced by protoporphyrin IX dimethyl ester, to a heme DNA aptamer, PS2.M, respectively, with a different rate constant. The heme transfer was further confirmed by the enhancement of peroxidase activity of the cyt b5s-PS2.M system due to the formation of catalytic PS2.M-heme comple...