% IMPORTANT: The following is UTF-8 encoded. This means that in the presence % of non-ASCII characters, it will not work with BibTeX 0.99 or older. % Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or % “biber”. @ARTICLE{Bommer:172577, author = {Bommer, Martin and Kunze, C. and Fesseler, J. and Schubert, T. and Diekert, G. and Dobbek, H.}, title = {{S}tructural basis for organohalide respiration}, journal = {Science}, volume = {346}, number = {6208}, issn = {1095-9203}, address = {Washington, DC [u.a.]}, publisher = {American Association for the Advancement of Science}, reportid = {PUBDB-2014-03806}, pages = {455-458}, year = {2014}, 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.}, cin = {DOOR / FS-PE}, ddc = {500}, cid = {I:(DE-H253)HAS-User-20120731 / I:(DE-H253)FS-PE-20120731}, pnm = {PETRA Beamline P11 (POF2-54G14)}, pid = {G:(DE-H253)POF2-P11-20130405}, experiment = {EXP:(DE-H253)P-P11-20150101}, typ = {PUB:(DE-HGF)16}, UT = {WOS:000343822900039}, pubmed = {pmid:25278505}, doi = {10.1126/science.1258118}, url = {https://bib-pubdb1.desy.de/record/172577}, }