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Wolinella succinogenes quinol:fumarate reductase and its comparison to E. coli succinate:quinone reductase
Author(s) -
Lancaster C.Roy D
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)01100-1
Subject(s) - fumarate reductase , reductase , chemistry , quinone , biochemistry , escherichia coli , stereochemistry , enzyme , succinate dehydrogenase , gene
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 Å 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.