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Production, crystallization and preliminary crystallographic analysis of Allochromatium vinosum thiosulfate dehydrogenase TsdA, an unusual acidophilic c ‐type cytochrome
Author(s) -
Brito José A.,
Gutierres André,
Denkmann Kevin,
Dahl Christiane,
Archer Margarida
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/s2053230x14019384
Subject(s) - tetrathionate , thiosulfate , sulfur , monoclinic crystal system , dehydrogenase , chemistry , crystallization , escherichia coli , crystallography , enzyme , biochemistry , organic chemistry , crystal structure , gene
The ability to perform the very simple oxidation of two molecules of thiosulfate to tetrathionate is widespread among prokaryotes. Despite the prevalent occurrence of tetrathionate formation and its well documented significance within the sulfur cycle, little is known about the enzymes that catalyze the oxidative condensation of two thiosulfate anions. To fill this gap, the thiosulfate dehydrogenase (TsdA) enzyme from the purple sulfur bacterium Allochromatium vinosum was recombinantly expressed in Escherichia coli , purified and crystallized, and a crystallographic data set was collected. The crystals belonged to the monoclinic space group C 2, with unit‐cell parameters a = 79.2, b = 69.9, c = 57.9 Å, β = 129.3°, contained one monomer per asymmetric unit and diffracted to a resolution of 1.98 Å.