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Wolinella succinogenes quinol-fumarate reductase and its comparison to E. coli succinate:quinone reductase

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Lancaster,  C. Roy D.
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Lancaster, C. R. D. (2003). Wolinella succinogenes quinol-fumarate reductase and its comparison to E. coli succinate:quinone reductase. FEBS Letters, 555(1), 21-28. doi:10.1016/s0014-5793(03)01100-1.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0024-DB71-5
Abstract
The three-dimensional structure of Wolinella succinogenes quinol:fumarate reductase (QFR), a dihaem-containing member of the superfamily of succinate:quinone oxidoreductases (SQOR), has been determined at 2.2 A resolution by X-ray crystallography [Lancaster et al., Nature 402 (1999) 377-385]. The structure and mechanism of W. succinogenes QFR and their relevance to the SQOR superfamily have recently been reviewed [Lancaster, Adv. Protein Chem. 63 (2003) 131-149]. Here, a comparison is presented of W. succinogenes QFR to the recently determined structure of the mono-haem containing succinate:quinone reductase from Escherichia coli [Yankovskaya et al., Science 299 (2003) 700-704]. In spite of differences in polypeptide and haem composition, the overall topology of the membrane anchors and their relative orientation to the conserved hydrophilic subunits is strikingly similar. A major difference is the lack of any evidence for a 'proximal' quinone site, close to the hydrophilic subunits, in W. succinogenes QFR.