| 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)
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