TY  - JOUR
AU  - Bommer, Martin
AU  - Kunze, C.
AU  - Fesseler, J.
AU  - Schubert, T.
AU  - Diekert, G.
AU  - Dobbek, H.
TI  - Structural basis for organohalide respiration
JO  - Science
VL  - 346
IS  - 6208
SN  - 1095-9203
CY  - Washington, DC [u.a.]
PB  - American Association for the Advancement of Science
M1  - PUBDB-2014-03806
SP  - 455-458
PY  - 2014
AB  - 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.
LB  - PUB:(DE-HGF)16
UR  - <Go to ISI:>//WOS:000343822900039
C6  - pmid:25278505
DO  - DOI:10.1126/science.1258118
UR  - https://bib-pubdb1.desy.de/record/172577
ER  -