| Item type |
デフォルトアイテムタイプ_（フル）(1) |
| 公開日 |
2023-03-18 |
| タイトル |
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タイトル |
Stabilization of Pseudomonas aeruginosa Cytochrome c551 by Systematic Amino Acid Substitutions Based on the Structure of Thermophilic Hydrogenobacter thermophilus Cytochrome c552 |
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言語 |
en |
| 作成者 |
Hasegawa, Jun
Shimahara, Hideto
Mizutani, Masayuki
Uchiyama, Susumu
Arai, Hiroyuki
Ishii, Masaharu
Kobayashi, Yuji
Ferguson, Stuart J.
Sambongi, Yoshihiro
Igarashi, Yasuo
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| アクセス権 |
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アクセス権 |
open access |
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アクセス権URI |
http://purl.org/coar/access_right/c_abf2 |
| 権利情報 |
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権利情報 |
This research was originally published in the Journal of Biological Chemistry. Jun Hasegawa, Hideto Shimahara, Masayuki Mizutani, Susumu Uchiyama, Hiroyuki Arai, Masaharu Ishii, Yuji Kobayashi, Stuart J. Ferguson, Yoshihiro Sambongi and Yasuo Igarashi. Stabilization of Pseudomonas aeruginosa Cytochrome c551 by Systematic Amino Acid Substitutions Based on the Structure of Thermophilic Hydrogenobacter thermophilus Cytochrome c552. J. Biol. Chem. 1999; 274(53):37533-37537. © the American Society for Biochemistry and Molecular Biology. |
| 内容記述 |
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内容記述 |
A heterologous overexpression system for mesophilic Pseudomonas aeruginosa holocytochrome c551 (PA c551) was established using Escherichia coli as a host organism. Amino acid residues were systematically substituted in three regions of PA c551 with the corresponding residues from thermophilic Hydrogenobacter thermophilus cytochrome c552 (HT c552), which has similar main chain folding to PA c551, but is more stable to heat. Thermodynamic properties of PA c551 with one of three single mutations (Phe-7 to Ala, Phe-34 to Tyr, or Val-78 to Ile) showed that these mutants had increased thermostability compared with that of the wild-type. Ala-7 and Ile-78 may contribute to the thermostability by tighter hydrophobic packing, which is indicated by the three dimensional structure comparison of PA c551 with HT c552. In the Phe-34 to Tyr mutant, the hydroxyl group of the Tyr residue and the guanidyl base of Arg-47 formed a hydrogen bond, which did not exist between the corresponding residues in HT c552. We also found that stability of mutant proteins to denaturation by guanidine hydrochloride correlated with that against the thermal denaturation. These results and others described here suggest that significant stabilization of PA c551 can be achieved through a few amino acid substitutions determined by molecular modeling with reference to the structure of HT c552. The higher stability of HT c552 may in part be attributed to some of these substitutions. |
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言語 |
en |
| 内容記述 |
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内容記述タイプ |
Other |
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内容記述 |
This work was supported in part by grants from the Japanese Ministry of Education, Science and Culture. |
| 出版者 |
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出版者 |
The American Society for Biochemistry and Molecular Biology, Inc. |
| 言語 |
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言語 |
eng |
| 資源タイプ |
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資源タイプ識別子 |
http://purl.org/coar/resource_type/c_6501 |
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資源タイプ |
journal article |
| 出版タイプ |
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出版タイプ |
VoR |
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出版タイプResource |
http://purl.org/coar/version/c_970fb48d4fbd8a85 |
| 関連情報 |
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識別子タイプ |
DOI |
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関連識別子 |
10.1074/jbc.274.53.37533 |
| 関連情報 |
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識別子タイプ |
PMID |
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関連識別子 |
10608805 |
| 関連情報 |
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識別子タイプ |
DOI |
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関連識別子 |
https://doi.org/10.1074/jbc.274.53.37533 |
| 収録物識別子 |
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収録物識別子タイプ |
ISSN |
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収録物識別子 |
0021-9258 |
| 収録物識別子 |
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収録物識別子タイプ |
ISSN |
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収録物識別子 |
1083-351X |
| 開始ページ |
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開始ページ |
37533 |
| 書誌情報 |
Journal of Biological Chemistry
Journal of Biological Chemistry
巻 274,
号 53,
p. 37533-37537,
発行日 1999-12-31
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| 旧ID |
48607 |
J. Biol. Chem_274_37533.pdf (158.1 KB)
