Physicochemical Properties of Diheme Cytochrome c4 of Unknown Function from Vibrio parahaemolyticus Strain RIMD2210633

Hideharu AKAZAKI; Yoshio FUTAMI; Naoya SHIBAYAMA; Ikuko SHIRASAKI; Harumi NAKADE; Hirotaka CHIDA; Wataru HAKAMATA; Sam-Yong PARK; Toshiyuki NISHIO; Tadatake OKU

doi:10.1271/bbb.80380

Biochemistry & Molecular Biology Notes

Physicochemical Properties of Diheme Cytochrome c₄ of Unknown Function from Vibrio parahaemolyticus Strain RIMD2210633

Hideharu AKAZAKI, Yoshio FUTAMI, Naoya SHIBAYAMA, Ikuko SHIRASAKI, Harumi NAKADE, Hirotaka CHIDA, Wataru HAKAMATA, Sam-Yong PARK, Toshiyuki NISHIO, Tadatake OKU

Author information

Hideharu AKAZAKI
Bio-Organic Chemistry Laboratory, Graduate School of Bioresource Sciences, Nihon University
Yoshio FUTAMI
Bio-Organic Chemistry Laboratory, Graduate School of Bioresource Sciences, Nihon University
Naoya SHIBAYAMA
Department of Physiology, Division of Biophysics, Jichi Medical School
Ikuko SHIRASAKI
Bio-Organic Chemistry Laboratory, Graduate School of Bioresource Sciences, Nihon University
Harumi NAKADE
Bio-Organic Chemistry Laboratory, Graduate School of Bioresource Sciences, Nihon University
Hirotaka CHIDA
Bio-Organic Chemistry Laboratory, Graduate School of Bioresource Sciences, Nihon University
Wataru HAKAMATA
Bio-Organic Chemistry Laboratory, Graduate School of Bioresource Sciences, Nihon University
Sam-Yong PARK
Protein Design Laboratory, Guraduate School of Integrated Science, Yokohama City University
Toshiyuki NISHIO
Bio-Organic Chemistry Laboratory, Graduate School of Bioresource Sciences, Nihon University
Tadatake OKU
Bio-Organic Chemistry Laboratory, Graduate School of Bioresource Sciences, Nihon University

Keywords: diheme cytochrome c₄, physicochemical property, recombinant protein, Vibrio parahaemolyticus

JOURNAL FREE ACCESS

2008 Volume 72 Issue 10 Pages 2791-2794

DOI https://doi.org/10.1271/bbb.80380

View "Advance Publication" version (October 7, 2008).

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Abstract

To characterize a diheme cytochrome c₄ of unknown functional of the Vibrio genus for the first time, the Vibrio parahaemolyticus cytochrome c₄ was overexpressed in Escherichia coli periplasm using the endogenous signal sequence. The physicochemical properties of the purified recombinant protein, viz., molecular mass, UV/Vis, and CD spectra, and the redox potentials of the N- and C-terminal domain hemes were determined.

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