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001     172577
005     20250730144658.0
024 7 _ |a 10.1126/science.1258118
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041 _ _ |a English
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100 1 _ |0 P:(DE-H253)PIP1019448
|a Bommer, Martin
|b 0
245 _ _ |a Structural basis for organohalide respiration
260 _ _ |a Washington, DC [u.a.]
|b American Association for the Advancement of Science
|c 2014
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|a Journal Article
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|a ARTICLE
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520 _ _ |a 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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700 1 _ |0 P:(DE-HGF)0
|a Kunze, C.
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700 1 _ |0 P:(DE-H253)PIP1020617
|a Fesseler, J.
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700 1 _ |0 P:(DE-HGF)0
|a Schubert, T.
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700 1 _ |0 P:(DE-HGF)0
|a Diekert, G.
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700 1 _ |0 P:(DE-HGF)0
|a Dobbek, H.
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|e Corresponding Author
773 _ _ |0 PERI:(DE-600)2066996-3
|a 10.1126/science.1258118
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|n 6208
|p 455-458
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|v 346
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|y 2014
856 4 _ |u http://www.sciencemag.org/content/early/2014/10/01/science.1258118.full.pdf
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