Functional characterization and membrane localization of the styrene oxide isomerase from <i>Rhodococcus opacus</i> 1CP and <i>Zavarzinia compransoris</i> Z-1155.

ABSTRACT: Styrene oxide isomerase (SOI) is a part of the styrene degradation enzyme complex, performing the isomerization of toxic intermediate styrene oxide into phenylacetaldehyde. For many years, the enzyme was believed to be cofactor-independent, and hence, the mechanism of this enzyme was proposed to be acid-base catalysis. Recently, the presence of heme was identified and reported in SOI from Pseudomonas sp. VLB120. Alongside, the membrane localization was also postulated since its discovery but lacks experimental proof. In this study, we highlight the localization of SOIs from two bacterial strains, Rhodococcus opacus 1CP and Zavarzinia compransoris Z-1155, heterologously overproduced in the cell membrane of E. coli via sfGFP-tagged fusions. In addition, the site-d

SUBMITTER: Kumaran S 

PROVIDER: S-EPMC12502698 | biostudies-literature | 2025 Oct

REPOSITORIES: biostudies-literature