Structural basis for organohalide respiration.

نویسندگان

  • Martin Bommer
  • Cindy Kunze
  • Jochen Fesseler
  • Torsten Schubert
  • Gabriele Diekert
  • Holger Dobbek
چکیده

Organohalide-respiring microorganisms can use a variety of persistent pollutants, including trichloroethene (TCE), as terminal electron acceptors. The final two-electron transfer step in organohalide respiration is catalyzed by reductive dehalogenases. Here we report the x-ray crystal structure of PceA, an archetypal dehalogenase from Sulfurospirillum multivorans, as well as structures of PceA in complex with TCE and product analogs. The active site harbors a deeply buried norpseudo-B12 cofactor within a nitroreductase fold, also found in a mammalian B12 chaperone. The structures of PceA reveal how a cobalamin supports a reductive haloelimination exploiting a conserved B12-binding scaffold capped by a highly variable substrate-capturing region.

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عنوان ژورنال:
  • Science

دوره 346 6208  شماره 

صفحات  -

تاریخ انتشار 2014