Active site rearrangement and structural divergence in prokaryotic respiratory oxidases
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- S. Safarian
- Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, D-60438 Frankfurt/Main, Germany.
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- A. Hahn
- Department of Structural Biology, Max Planck Institute of Biophysics, D-60438 Frankfurt/Main, Germany.
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- D. J. Mills
- Department of Structural Biology, Max Planck Institute of Biophysics, D-60438 Frankfurt/Main, Germany.
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- M. Radloff
- Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, D-60438 Frankfurt/Main, Germany.
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- M. L. Eisinger
- Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, D-60438 Frankfurt/Main, Germany.
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- A. Nikolaev
- Laboratoire de Bioélectrochimie et Spectroscopie, UMR 7140, Chimie de la Matière Complexe, Université de Strasbourg-CNRS, 67000 Strasbourg, France.
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- J. Meier-Credo
- Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, D-60438 Frankfurt/Main, Germany.
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- F. Melin
- Laboratoire de Bioélectrochimie et Spectroscopie, UMR 7140, Chimie de la Matière Complexe, Université de Strasbourg-CNRS, 67000 Strasbourg, France.
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- H. Miyoshi
- Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan.
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- R. B. Gennis
- Department of Biochemistry, University of Illinois, Urbana, IL 61801, USA.
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- J. Sakamoto
- Department of Bioscience and Bioinformatics, Kyushu Institute of Technology, Kawazu 680-4, Iizuka, Fukuoka-ken 820-8502, Japan.
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- J. D. Langer
- Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, D-60438 Frankfurt/Main, Germany.
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- P. Hellwig
- Laboratoire de Bioélectrochimie et Spectroscopie, UMR 7140, Chimie de la Matière Complexe, Université de Strasbourg-CNRS, 67000 Strasbourg, France.
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- W. Kühlbrandt
- Department of Structural Biology, Max Planck Institute of Biophysics, D-60438 Frankfurt/Main, Germany.
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- H. Michel
- Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, D-60438 Frankfurt/Main, Germany.
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説明
<jats:title>Hemes switch spots in a terminal oxidase</jats:title> <jats:p> Reduction of molecular oxygen to water is the driving force for respiration in aerobic organisms and is catalyzed by several distinct integral membrane complexes. These include an exclusively prokaryotic enzyme, cytochrome bd–type quinol oxidase, which is a potential antimicrobial target. Safarian <jats:italic>et al.</jats:italic> determined a high-resolution cryo–electron microscopy structure of this enzyme from the enteric bacterium <jats:italic>Escherichia coli</jats:italic> . Comparison to a homolog reveals a complete relocation of the site of oxygen binding and reduction caused by a change in the arrangement of heme cofactors and channels in the protein scaffold. This switch illustrates the diversity of structure and function in this family of enzymes and might reflect different biochemical roles of these homologs. </jats:p> <jats:p> <jats:italic>Science</jats:italic> , this issue p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6461" page="100" related-article-type="in-this-issue" vol="366" xlink:href="10.1126/science.aay0967">100</jats:related-article> </jats:p>
収録刊行物
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- Science
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Science 366 (6461), 100-104, 2019-10-04
American Association for the Advancement of Science (AAAS)
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キーワード
- Models, Molecular
- Ubiquinone
- Escherichia coli Proteins
- Cryoelectron Microscopy
- Heme
- Cytochrome b Group
- Oxygen
- Protein Subunits
- Electron Transport Chain Complex Proteins
- Catalytic Domain
- Escherichia coli
- [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology
- Protons
- Oxidoreductases
- Protein Structure, Quaternary
- Oxidation-Reduction
詳細情報 詳細情報について
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- CRID
- 1361418519481400576
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- ISSN
- 10959203
- 00368075
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- PubMed
- 31604309
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- データソース種別
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- Crossref
- OpenAIRE