In:
Science, American Association for the Advancement of Science (AAAS), Vol. 346, No. 6208 ( 2014-10-24), p. 455-458
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-B 12 cofactor within a nitroreductase fold, also found in a mammalian B 12 chaperone. The structures of PceA reveal how a cobalamin supports a reductive haloelimination exploiting a conserved B 12 -binding scaffold capped by a highly variable substrate-capturing region.
Type of Medium:
Online Resource
ISSN:
0036-8075
,
1095-9203
DOI:
10.1126/science.1258118
Language:
English
Publisher:
American Association for the Advancement of Science (AAAS)
Publication Date:
2014
detail.hit.zdb_id:
128410-1
detail.hit.zdb_id:
2066996-3
detail.hit.zdb_id:
2060783-0
SSG:
11
Bookmarklink