Fumarate reductase: Structural and mechanistic insights from the catalytic reduction of 2-methylfumarate

Caroline Wardrope, Christopher Mowat, Malcolm Walkinshaw, Graeme Reid, Stephen Chapman

Research output: Contribution to journalArticlepeer-review

Abstract

The soluble fumarate reductase (FR) from Shewanella frigidimarina can catalyse the reduction of 2-methylfumarate with a kcat of 9.0 s−1 and a KM of 32 μM. This produces the chiral molecule 2-methylsuccinate. Here, we present the structure of FR to a resolution of 1.5 Å with 2-methylfumarate bound at the active site. The mode of binding of 2-methylfumarate allows us to predict the stereochemistry of the product as (S)-2-methylsuccinate. To test this prediction we have analysed the product stereochemistry by circular dichroism spectroscopy and confirmed the production of (S)-2-methylsuccinate.
Original languageEnglish
Pages (from-to)1677-1680
Number of pages4
JournalFEBS Letters
Volume580
Issue number6
Early online date17 Feb 2006
DOIs
Publication statusPublished - 2006

Keywords / Materials (for Non-textual outputs)

  • Fumerate reductase
  • Flavocytochrome
  • c3
  • 2-Methylfumerate
  • Mesaconate
  • 2-Methylsuccinate

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