A cytosolic cytochrome b5-like protein in yeast cell accelerating the electron transfer from NADPH to cytochrome c catalyzed by Old Yellow Enzyme

被引：1

作者：

Nakagawa, M

Yamano, T

Kuroda, K

Nonaka, Y

Tojo, H

Fujii, S ^{[1
]}

机构：

[1] Kansai Med Univ, Chem Lab, Hirakata, Osaka 5731136, Japan

[2] Koshien Univ, Coll Nutr, Takarazuka, Hyogo 6650006, Japan

[3] Osaka Univ, Grad Sch Med, Dept Biochem & Mol Biol, Suita, Osaka 5650871, Japan

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2005年 / 338卷 / 01期

关键词：

cytochrome b(5); cytochrome b(5)-like protein; Old Yellow Enzyme; electron transfer; Saccharomyces cerevisiae; MALDI-TOF/MS;

D O I：

10.1016/j.bbrc.2005.09.033

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A 410-nm absorbing species which enhanced the reduction rate of cytochrome c by Old Yellow Enzyme (OYE) with NADPH was found in Saccharomyces cerevisiae. It was solubilized together with OYE by the treatment of yeast cells with 10% ethyl acetate. The purified species showed visible absorption spectra in both oxidized and reduced forms, which were the same as those of the yeast microsomal cytochrome b(5). At least 14 amino acid residues of the N-terminal region coincided with those of yeast microsomal b(5), but the protein had a lower molecular weight determined to be 12,600 by SDS-PAGE and 9775 by mass spectrometry. The cytochroine b(5)-like protein enhanced the reduction rate of cytochrome c by OYE, and a plot of the reduction rates against its concentration showed a sigmoidal Curve with an inflexion point at 6 x 10(-8) M of the protein. (c) 2005 Elsevier Inc. All rights reserved.

引用

页码：605 / 609

页数：5