Structural basis for organohalide respiration

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 P...

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Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 2014-10, Vol.346 (6208), p.455-458
Main Authors: Bommer, Martin, Kunze, Cindy, Fesseler, Jochen, Schubert, Torsten, Diekert, Gabriele, Dobbek, Holger
Format: Article
Language:English
Subjects:
Anaerobiosis
Bacteria
Bacterial Proteins - chemistry
Breaking down
Catalytic Domain
Crystal structure
Crystallography, X-Ray
Electron Transport
Enzymes
Epsilonproteobacteria - enzymology
Microorganisms
Oxidoreductases - chemistry
Pollutants
Protein Folding
Protein Structure, Secondary
Protein Structure, Tertiary
Respiration
Substrate Specificity
Trichloroethylene
Trichloroethylene - chemistry
Vitamin B 12 - chemistry
X-rays
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Summary: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.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.1258118