%0 Journal Article
%A Bommer, Martin
%A Kunze, C.
%A Fesseler, J.
%A Schubert, T.
%A Diekert, G.
%A Dobbek, H.
%T Structural basis for organohalide respiration
%J Science
%V 346
%N 6208
%@ 1095-9203
%C Washington, DC [u.a.]
%I American Association for the Advancement of Science
%M PUBDB-2014-03806
%P 455-458
%D 2014
%X 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.
%F PUB:(DE-HGF)16
%9 Journal Article
%U <Go to ISI:>//WOS:000343822900039
%$ pmid:25278505
%R 10.1126/science.1258118
%U https://bib-pubdb1.desy.de/record/172577