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Crystallization and preliminary X‐ray crystallographic studies of the ArsI C–As lyase from Thermomonospora curvata
Author(s) -
Nadar S. Venkadesh,
Yoshinaga Masafumi,
Kandavelu Palani,
Sankaran Banumathi,
Rosen Barry P.
Publication year - 2014
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x14008814
Subject(s) - biotransformation , arsenic , arsenite , chemistry , arsenate , lyase , biogeochemical cycle , thermophile , stereochemistry , extremophile , crystallization , enantiomer , biochemistry , environmental chemistry , enzyme , organic chemistry
Arsenic is a ubiquitous and carcinogenic environmental element that enters the biosphere primarily from geochemical sources, but also through anthropogenic activities. Microorganisms play an important role in the arsenic biogeochemical cycle by biotransformation of inorganic arsenic into organic arsenicals and vice versa . ArsI is a microbial nonheme ferrous‐dependent dioxygenase that transforms toxic methylarsonous acid to the less toxic inorganic arsenite by C–As bond cleavage. An ArsI ortholog from the thermophilic bacterium Thermomonospora curvata was expressed, purified and crystallized. The crystals diffracted to 1.46 Å resolution and belonged to space group P 4 3 2 1 2 or its enantiomer P 4 1 2 1 2, with unit‐cell parameters a = b = 42.2, c = 118.5 Å.