Heterologously expressed arsenite oxidase: A system to study biogenesis and structure/function relationships of the enzyme family

► We expressed the arsenite oxidase from Ralstonia sp. S22 in Escherichia coli. ► Results on wild type and mutated Aio pertaining to the biogenesis of the enzyme were obtained. ► We analyzed Aio's structure/function relationships by comparing wild type and mutant enzymes. ► We propose that the uncleaved Tat sequence of AioB anchors the enzyme to the membrane. ► The S-S bridge in the Rieske protein affects neither redox nor structural/functional properties.