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 >

A novel membrane-anchored cytochrome c-550 of alkaliphilic Bacillus clarkii K24-1U: expression, molecular features and properties of redox potential

Files in This Item:
13-3_p491-504.pdf420.77 kBPDFView/Open
Please use this identifier to cite or link to this item:http://hdl.handle.net/2115/38565

Title: A novel membrane-anchored cytochrome c-550 of alkaliphilic Bacillus clarkii K24-1U: expression, molecular features and properties of redox potential
Authors: Ogami, Shinichi Browse this author
Hijikata, Shoichi Browse this author
Tsukahara, Tamotsu Browse this author
Mie, Yasuhiro Browse this author
Matsuno, Toshihide Browse this author
Morita, Naoki Browse this author
Hara, Isao Browse this author
Yamazaki, Koji Browse this author
Inoue, Norio Browse this author
Yokota, Atsushi Browse this author →KAKEN DB
Hoshino, Tamotsu Browse this author
Yoshimune, Kazuaki Browse this author
Yumoto, Isao Browse this author
Keywords: Alkaliphilic
Bacillus clarkii
Cytochrome c
Expression
Posttranslational modification
Membrane-anchored
Midpoint redox potential
Issue Date: May-2009
Publisher: Springer Japan
Journal Title: Extremophiles
Volume: 13
Issue: 3
Start Page: 491
End Page: 504
Publisher DOI: 10.1007/s00792-009-0234-6
Abstract: A membrane-anchored cytochrome c-550, which is highly expressed in obligately alkaliphilic Bacillus clarkii K24-1U, was purified and characterized. The protein contained a conspicuous sequence of Gly22-Asn34, in comparison with the other Bacillus small cytochromes c. Analytical data indicated that the original and lipase-treated intermediate forms of cytochrome c-550 bind to fatty acids of C15, C16 and C17 chain lengths and C15 chain length, respectively, and it was considered that these fatty acids are bound to glycerol-Cys18. Since there was a possibility that the presence of a diacylglycerol anchor contributed to the formation of dimeric states of this protein (20 and 17 kDa in SDS-PAGE), a C18M (Cys18 → Met)-cytochrome c-550 was constructed. The molecular mass of the C18M-cytochrome c-550 was determined as 15 and 10 kDa in SDS-PAGE and 23 kDa in blue native PAGE. The C18M-cytochrome c-550 bound with or without Triton X-100 formed a tetramer as the original cytochrome c-550 bound with Triton X-100, as determined by gel filtration. The midpoint redox potential of cytochrome c-550 as determined by redox titration was +83 mV, while that determined by cyclic voltammetric measurement was +7 mV. The above results indicate that cytochrome c-550 is a novel cytochrome c.
Rights: The original publication is available at www.springerlink.com
Type: article (author version)
URI: http://hdl.handle.net/2115/38565
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 )

MathJax is now OFF:


 

 - Hokkaido University