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Stabilization of Pseudomonas aeruginosa Cytochrome c551 by Systematic Amino Acid Substitutions Based on the Structure of Thermophilic Hydrogenobacter thermophilus Cytochrome c552

https://hiroshima.repo.nii.ac.jp/records/2007229
https://hiroshima.repo.nii.ac.jp/records/2007229
af9fa881-23d2-45c3-a542-a87f417c78c5
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J. J. Biol. Chem_274_37533.pdf (158.1 KB)
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
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
言語 en
作成者 Hasegawa, Jun

× Hasegawa, Jun

en Hasegawa, Jun

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Shimahara, Hideto

× Shimahara, Hideto

en Shimahara, Hideto

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Mizutani, Masayuki

× Mizutani, Masayuki

en Mizutani, Masayuki

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Uchiyama, Susumu

× Uchiyama, Susumu

en Uchiyama, Susumu

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Arai, Hiroyuki

× Arai, Hiroyuki

en Arai, Hiroyuki

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Ishii, Masaharu

× Ishii, Masaharu

en Ishii, Masaharu

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Kobayashi, Yuji

× Kobayashi, Yuji

en Kobayashi, Yuji

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Ferguson, Stuart J.

× Ferguson, Stuart J.

en Ferguson, Stuart J.

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Sambongi, Yoshihiro

× Sambongi, Yoshihiro

en Sambongi, Yoshihiro

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Igarashi, Yasuo

× Igarashi, Yasuo

en Igarashi, Yasuo

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アクセス権
アクセス権 open access
アクセス権URI http://purl.org/coar/access_right/c_abf2
権利情報
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
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.
言語 en
内容記述
内容記述タイプ Other
内容記述 This work was supported in part by grants from the Japanese Ministry of Education, Science and Culture.
出版者
出版者 The American Society for Biochemistry and Molecular Biology, Inc.
言語
言語 eng
資源タイプ
資源タイプ識別子 http://purl.org/coar/resource_type/c_6501
資源タイプ journal article
出版タイプ
出版タイプ VoR
出版タイプResource http://purl.org/coar/version/c_970fb48d4fbd8a85
関連情報
識別子タイプ DOI
関連識別子 10.1074/jbc.274.53.37533
関連情報
識別子タイプ PMID
関連識別子 10608805
関連情報
識別子タイプ DOI
関連識別子 https://doi.org/10.1074/jbc.274.53.37533
収録物識別子
収録物識別子タイプ ISSN
収録物識別子 0021-9258
収録物識別子
収録物識別子タイプ ISSN
収録物識別子 1083-351X
開始ページ
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
旧ID 48607
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