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  The role of tryptophan 272 in the Paracoccus denitrificans cytochrome c oxidase

MacMillan, F., Budiman, K., Angerer, H., & Michel, H. (2006). The role of tryptophan 272 in the Paracoccus denitrificans cytochrome c oxidase. FEBS Letters, 580(5), 1345-1349. doi:10.1016/j.febslet.2006.01.054.

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資料種別: 学術論文

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 作成者:
MacMillan, Fraser1, 著者
Budiman, Kerstin2, 著者           
Angerer, Heike2, 著者           
Michel, Hartmut2, 著者                 
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1Institut für Physikalische and Theoretische Chemie, Center for Biomolecular Magnetic Resonance, Johann Wolfgang Goethe-Universität, Frankfurt D-60439, Frankfurt am Main, Germany, ou_persistent22              
2Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              

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キーワード: Cytochrome c oxidase; Tyrosine radical; Variants; Electron paramagnetic; resonance spectroscopy; Bioenergetics
 要旨: The mechanism of electron coupled proton transfer in cytochrome c oxidase (CcO) is still poorly understood. The PM-intermediate of the catalytic cycle is an oxoferryl state whose generation requires one additional electron, which cannot be provided by the two metal centres. The missing electron has been suggested to be donated to this binuclear site by a tyrosine residue. A tyrosine radical species has been detected in the PM and Fradical dot intermediates (formed by addition of H2O2) of the Paraccocus denitrificans CcO using electron paramagnetic resonance (EPR) spectroscopy. From the study of conserved variants its origin was determined to be Y167 which is surprising as this residue is not part of the active site. Upon inspection of the active site it becomes evident that W272 could be the actual donor of the missing electron, which can then be replenished from Y167 or from the Y280-H276 cross link in the natural cycle. To address the question, whether such a direct electron transfer pathway to the binuclear centre exists two tryptophan 272 variants in subunit I have been generated. These variants are characterised by their turnover rates as well as using EPR and optical spectroscopy. From these experiments it is concluded, that W272 is an important intermediate in the formation of the radical species appearing in PM and Fradical dot intermediates produced with hydrogen peroxide. The significance of this finding for the catalytic function of the enzyme is discussed.

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言語: eng - English
 日付: 2006-01-182005-12-082006-01-182006-01-262006-02-20
 出版の状態: 出版
 ページ: 5
 出版情報: -
 目次: -
 査読: 査読あり
 識別子(DOI, ISBNなど): DOI: 10.1016/j.febslet.2006.01.054
 学位: -

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出版物 1

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出版物名: FEBS Letters
  その他 : FEBS Lett.
種別: 学術雑誌
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出版社, 出版地: Amsterdam : Elsevier
ページ: - 巻号: 580 (5) 通巻号: - 開始・終了ページ: 1345 - 1349 識別子(ISBN, ISSN, DOIなど): ISSN: 0014-5793
CoNE: https://pure.mpg.de/cone/journals/resource/954925399501