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  1. 学術雑誌論文
  2. 4 自然科学

Mutation Analysis of the Interaction of B-type Cytochrome c Oxidase with its Natural Substrate Cytochrome c-551

http://hdl.handle.net/10228/4692
http://hdl.handle.net/10228/4692
6c7f608e-a870-47c5-80db-755ba5476eed
名前 / ファイル ライセンス アクション
j.jbiosc.2009.10.008.pdf j.jbiosc.2009.10.008.pdf (222.1 kB)
アイテムタイプ 学術雑誌論文 = Journal Article(1)
公開日 2010-07-13
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
タイトル
タイトル Mutation Analysis of the Interaction of B-type Cytochrome c Oxidase with its Natural Substrate Cytochrome c-551
言語
言語 eng
著者 Kabashima, Yoshiki

× Kabashima, Yoshiki

WEKO 14077

Kabashima, Yoshiki

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Ueda, Naoaki

× Ueda, Naoaki

WEKO 14078

Ueda, Naoaki

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Sone, Nobuhito

× Sone, Nobuhito

WEKO 14079

Sone, Nobuhito

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坂本, 順司

× 坂本, 順司

WEKO 14076
e-Rad 80175364
Scopus著者ID 7103305874
九工大研究者情報 271

en Sakamoto, Junshi

ja 坂本, 順司

ja-Kana サカモト, ジュンシ


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抄録
内容記述タイプ Abstract
内容記述 Heme-copper oxidases in the respiratory chain are classified into three subfamilies: A-, B- and C-types. Cytochrome bo3-type cytochrome c oxidase from thermophilic Bacillus is a B-type oxidase that is thought to interact with cytochrome c through hydrophobic interactions. This is in contrast to A-type oxidases, which bind cytochrome c molecules primarily through electrostatic forces between acidic residues in the oxidase subunit II and basic residues within cytochromes. In order to investigate the substrate-binding site in cytochrome bo3, eight acidic residues in subunit II were mutated to corresponding neutral residues and enzymatic activity was measured using cytochrome c-551 from closely related Bacillus PS3. The mutation of E116, located at the interface to subunit I, decreased the kcat value most prominently without affecting the Km value, indicating that the residue is important for electron transfer. The mutation of D99, located close to the CuA site, largely affected both values, suggesting that it is important for both electron transfer and substrate binding. The mutation of D49 and E84 did not affect enzyme kinetic parameters, but the mutation of E64, E66 and E68 lowered the affinity of cytochrome bo3 for cytochrome c-551 without affecting the kcat value. These three residues are located at the front of the hydrophilic globular domain and distant from the CuA site, suggesting that these amino acids compose an acidic patch for a second substrate-binding site. This is the first report on site-directed mutagenesis experiments of a B-type heme-copper oxidase.
書誌情報 Journal of Bioscience and Bioengineering

巻 109, 号 4, p. 325-330, 発行日 2010-04
出版社
出版者 社団法人日本生物工学会
DOI
関連タイプ isVersionOf
識別子タイプ DOI
関連識別子 info:doi/10.1016/j.jbiosc.2009.10.008
ISSN
収録物識別子タイプ ISSN
収録物識別子 1389-1723
ISSN
収録物識別子タイプ ISSN
収録物識別子 1347-4421
著作権関連情報
権利情報 Copyright (c) 2009 The Society for Biotechnology, Japan Published by Elsevier B.V.
キーワード
主題Scheme Other
主題 Geobacillus thermodenitrificans
キーワード
主題Scheme Other
主題 B-type heme-copper oxidase
キーワード
主題Scheme Other
主題 bo3-type cytochrome c oxidase
キーワード
主題Scheme Other
主題 Cytochrome c-551
キーワード
主題Scheme Other
主題 Thermophilic bacteria
出版タイプ
出版タイプ AM
出版タイプResource http://purl.org/coar/version/c_ab4af688f83e57aa
査読の有無
値 yes
研究者情報
URL https://hyokadb02.jimu.kyutech.ac.jp/html/271_ja.html
連携ID
値 35
業績ID
値 123466CD9853DAE549257704001CDF53
情報源
識別子タイプ DOI
関連識別子 https://doi.org/10.1016/j.jbiosc.2009.10.008
関連名称 https://doi.org/10.1016/j.jbiosc.2009.10.008
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