Open AccessA rs H from S ynechocystis sp. PCC 6803 reduces chromate and ferric iron
Author(s) -
Xue XiMei,
Yan Yu,
Xu HuiJuan,
Wang Ning,
Zhang Xiao,
Ye Jun
Publication year - 2014
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/1574-6968.12481
Subject(s) - chromate conversion coating , arsenic , synechocystis , arsenite , arsenate , chromium , ferric , chemistry , bacteria , biochemistry , microbiology and biotechnology , biology , inorganic chemistry , gene , organic chemistry , genetics , mutant
A rs H is widely distributed in bacteria, and its function remains to be characterized. In this study, we investigated the function of A rs H from S ynechocystis sp. PCC 6803. The inactivation of ars H by insertion of a kanamycin‐resistance gene in S ynechocystis sp. PCC 6803 resulted in the decrease of arsenic and chromium accumulation compared with the wild type. A rs H expression in E scherichia coli strain R osetta increased its resistance to chromate by reducing chromate in the medium and cells to chromium ( III ). In addition, A rs H in R osetta conferred resistance to arsenic. The purified S ynechocystis A rs H was able to reduce chromate and ferric iron at the expense of NADPH . Nonlinear regression values of K 0.5 for chromate and ferric iron were 71.9 ± 17.8 μM and 59.3 ± 13.8 μM, respectively. The expression level of ars H was induced by arsenite and arsenate, but not chromate or ferric iron. Our results suggest that S ynechocystis A rs H had no substrate specificities and shared some biochemical properties that other enzymes possessed. A rs H may be involved in coordinating oxidative stress response generated by arsenic.