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Title: A cytosolic cytochrome b {sub 5}-like protein in yeast cell accelerating the electron transfer from NADPH to cytochrome c catalyzed by Old Yellow Enzyme

Abstract

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 {sub 5}. At least 14 amino acid residues of the N-terminal region coincided with those of yeast microsomal b {sub 5}, but the protein had a lower molecular weight determined to be 12,600 by SDS-PAGE and 9775 by mass spectrometry. The cytochrome b {sub 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{sup -8} M of the protein.

Authors:
 [1];  [1];  [1];  [2];  [3];  [4]
  1. Laboratory of Chemistry, Kansai Medical University, Hirakata 573-1136 (Japan)
  2. College of Nutrition, Koshien University, Takarazuka 665-0006 (Japan)
  3. Department of Biochemistry and Molecular Biology, Osaka University Graduate School of Medicine, Suita 565-0871 (Japan)
  4. Laboratory of Chemistry, Kansai Medical University, Hirakata 573-1136 (Japan). E-mail: fujii@makino.kmu.ac.jp
Publication Date:
OSTI Identifier:
20793213
Resource Type:
Journal Article
Resource Relation:
Journal Name: Biochemical and Biophysical Research Communications; Journal Volume: 338; Journal Issue: 1; Other Information: DOI: 10.1016/j.bbrc.2005.09.033; PII: S0006-291X(05)02045-0; Copyright (c) 2005 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; ABSORPTION SPECTRA; ACETATES; AMINO ACIDS; ELECTRON TRANSFER; ENZYMES; MASS SPECTROSCOPY; MOLECULAR WEIGHT; REDUCTION; SACCHAROMYCES CEREVISIAE

Citation Formats

Nakagawa, Manabu, Yamano, Toshio, Kuroda, Kiyo, Nonaka, Yasuki, Tojo, Hiromasa, and Fujii, Shigeru. A cytosolic cytochrome b {sub 5}-like protein in yeast cell accelerating the electron transfer from NADPH to cytochrome c catalyzed by Old Yellow Enzyme. United States: N. p., 2005. Web. doi:10.1016/J.BBRC.2005.0.
Nakagawa, Manabu, Yamano, Toshio, Kuroda, Kiyo, Nonaka, Yasuki, Tojo, Hiromasa, & Fujii, Shigeru. A cytosolic cytochrome b {sub 5}-like protein in yeast cell accelerating the electron transfer from NADPH to cytochrome c catalyzed by Old Yellow Enzyme. United States. doi:10.1016/J.BBRC.2005.0.
Nakagawa, Manabu, Yamano, Toshio, Kuroda, Kiyo, Nonaka, Yasuki, Tojo, Hiromasa, and Fujii, Shigeru. Fri . "A cytosolic cytochrome b {sub 5}-like protein in yeast cell accelerating the electron transfer from NADPH to cytochrome c catalyzed by Old Yellow Enzyme". United States. doi:10.1016/J.BBRC.2005.0.
@article{osti_20793213,
title = {A cytosolic cytochrome b {sub 5}-like protein in yeast cell accelerating the electron transfer from NADPH to cytochrome c catalyzed by Old Yellow Enzyme},
author = {Nakagawa, Manabu and Yamano, Toshio and Kuroda, Kiyo and Nonaka, Yasuki and Tojo, Hiromasa and Fujii, Shigeru},
abstractNote = {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 {sub 5}. At least 14 amino acid residues of the N-terminal region coincided with those of yeast microsomal b {sub 5}, but the protein had a lower molecular weight determined to be 12,600 by SDS-PAGE and 9775 by mass spectrometry. The cytochrome b {sub 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{sup -8} M of the protein.},
doi = {10.1016/J.BBRC.2005.0},
journal = {Biochemical and Biophysical Research Communications},
number = 1,
volume = 338,
place = {United States},
year = {Fri Dec 09 00:00:00 EST 2005},
month = {Fri Dec 09 00:00:00 EST 2005}
}