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  Insights from the structure of the yeast cytochrome bc1 complex: crystallization of membrane proteins with antibody fragments

Hunte, C. (2001). Insights from the structure of the yeast cytochrome bc1 complex: crystallization of membrane proteins with antibody fragments. FEBS Letters, 504(3), 126-132. doi:10.1016/S0014-5793(01)02744-2.

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 Creators:
Hunte, Carola1, Author           
Affiliations:
1Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              

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Free keywords: Oxidoreductase; Complex III; Antibody fragment; Crystallization; Q cycle; Quinol
 Abstract: Abstract

The ubiquinol:cytochrome c oxidoreductase (EC 1.20.2.2, QCR or cytochrome bc1 complex) is a component of respiratory and photosynthetic electron transfer chains in mitochondria and bacteria. The complex transfers electrons from quinol to cytochrome c. Electron transfer is coupled to proton translocation across the lipid bilayer, thereby generating an electrochemical proton gradient, which conserves the free energy of the redox reaction. The yeast complex was crystallized with antibody Fv fragments, a promising technique to obtain well-ordered crystals from membrane proteins. The high-resolution structure of the yeast protein reveals details of the catalytic sites of the complex, which are important for electron and proton transfer.

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Language(s): eng - English
 Dates: 2001-07-112001-07-212001-08-282001-08-31
 Publication Status: Issued
 Pages: 7
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/S0014-5793(01)02744-2
 Degree: -

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Title: FEBS Letters
  Other : FEBS Lett.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: 504 (3) Sequence Number: - Start / End Page: 126 - 132 Identifier: ISSN: 0014-5793
CoNE: https://pure.mpg.de/cone/journals/resource/954925399501