HUSCAP logo Hokkaido Univ. logo

Hokkaido University Collection of Scholarly and Academic Papers >
Graduate School of Agriculture / Faculty of Agriculture >
Peer-reviewed Journal Articles, etc >

Cytochrome c-552 from Gram-Negative Alkaliphilic Pseudomonas alcaliphila AL15-21T Alters the Redox Properties at High pH

Files in This Item:
JBB103-3.pdf281.88 kBPDFView/Open
Please use this identifier to cite or link to this item:

Title: Cytochrome c-552 from Gram-Negative Alkaliphilic Pseudomonas alcaliphila AL15-21T Alters the Redox Properties at High pH
Authors: Matsuno, Toshihide Browse this author
Morishita, Nozomu Browse this author
Yamazaki, Koji Browse this author
Inoue, Norio Browse this author
Sato, Yukari Browse this author
Ichise, Nobutoshi Browse this author
Hara, Isao Browse this author
Hoshino, Tamotsu Browse this author
Matsuyama, Hidetoshi Browse this author
Yoshimune, Kazuaki Browse this author
Yumoto, Isao Browse this author
Keywords: alkaliphilic
Pseudomonas alcaliphila
cytochrome c
redox potential
Issue Date: Mar-2007
Publisher: Society for Biotechnology, Japan
Journal Title: Journal of Bioscience and Bioengineering
Volume: 103
Issue: 3
Start Page: 247
End Page: 254
Publisher DOI: 10.1263/jbb.103.247
Abstract: A soluble class I cytochrome c of an alkaliphile was purified and characterized, and its primary structure was determined. This is the first example of a soluble class I cytochrome c in alkaliphiles. Cells the alkaliphilic gram-negative bacterium Pseudomonas alcaliphila AL15-21T grown at pH 10 had a soluble cytochrome c content that was more than twofold that of strain AL15-21T cells grown at pH 7 under air-limited conditions. Cytochrome c-552, a soluble cytochrome c with a low molecular weight, was purified from strain AL15-21T cells grown at pH 10 under air-limited conditions. Cytochrome c-552 had a molecular mass of 7.5 kDa and exhibited an almost fully reduced state in the resting form, which exhibited absorption maxima at wavelengths of 552, 523 and 417 nm. In the oxidized state, it exhibited an absorption maximum at 412 nm when it was oxidized by ferricyanide, its isoelectric point (pI) was 4.3 and it contained one heme c as a prosthetic group. Cytochrome c-552 was autoreduced at pH 10, and the autoreduction was reproducible. On the other hand, the autoreduction of cytochrome c-552 was not observed at pH 7.0. When pH was increased from 7.0 to 8.3, its midpoint redox potentials (Em values) increased from +228 mV to +276 mV as determined by redox titrations, and from +217 mV to +275 mV as determined by cyclic voltammetric measurements. The amino acid sequence deduced by cytochrome c-552 gene analysis revealed that the sequence consists of 96 residues, including 19 residues as an amino-terminal signal peptide. A phylogenetic tree based on amino acid sequence indicated that the protein belongs to group 4, cytochrome c5 in class I cytochrome c.
Type: article (author version)
Appears in Collections:農学院・農学研究院 (Graduate School of Agriculture / Faculty of Agriculture) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 湯本 勲

Export metadata:

OAI-PMH ( junii2 , jpcoar_1.0 )

MathJax is now OFF:


 - Hokkaido University