Journal Article PUBDB-2014-03806

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Structural basis for organohalide respiration

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2014
American Association for the Advancement of Science Washington, DC [u.a.]

Science 346(6208), 455-458 () [10.1126/science.1258118]
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Abstract: 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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Contributing Institute(s):
  1. DOOR-User (DOOR)
  2. Experimentebetreuung PETRA III (FS-PE)
Research Program(s):
  1. PETRA Beamline P11 (POF2-54G14) (POF2-54G14)
Experiment(s):
  1. PETRA Beamline P11 (PETRA III)

Appears in the scientific report 2014
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 Record created 2014-10-15, last modified 2025-07-30


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