Open AccessEnzymes responsible for chlorate reduction by Pseudomonas sp. are different from those used for perchlorate reduction by Azospira sp.
Author(s) -
Steinberg Lisa M.,
Trimble John J.,
Logan Bruce E.
Publication year - 2005
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 - 10.1016/j.femsle.2005.05.003
Subject(s) - chlorate , perchlorate , biochemistry , enzyme , reductase , nitrate reductase , chemistry , protein subunit , biology , inorganic chemistry , organic chemistry , gene , ion
Pseudomonas sp. PDA is an unusual bacterium due to its ability to respire using chlorate under aerobic conditions. The chlorate reductase produced by PDA was shown to be intrinsically different from the enzyme responsible for chlorate and perchlorate [(per)chlorate] reduction produced by Azospira sp. KJ based on subunit composition and other enzyme properties. The perchlorate reductase from strain KJ appeared to have two subunits (100 and 40 kDa) while the chlorate reductase from PDA had three subunits (60, 48, and 27 kDa). N‐terminal amino acid sequencing of the 100 kDa protein from strain KJ showed a 77% similarity with the perchlorate reductase alpha subunit from another perchlorate‐respiring bacterium, Dechloromonas agitata , while the N‐terminus amino acid sequence of the 60 kDa protein from strain PDA did not show a similarity to previously isolated chlorate or perchlorate reductases.