Related Experiment Video
Updated: Aug 13, 2026

Anaerobic Protein Purification and Kinetic Analysis via Oxygen Electrode for Studying DesB Dioxygenase Activity and Inhibition
Published on: October 3, 2018
Identification and characterization of a novel bacterial sulfite oxidase with no heme binding domain from Deinococcus
Giovanni D'Errico1, Anna Di Salle, Francesco La Cara
1Istituto di Biochimica delle Proteine, CNR, via Pietro Castellino 111, 80131 Naples, Italy.
Abstract:
An open reading frame (draSO) encoding a putative sulfite oxidase (SO) was identified in the sequence of chromosome II of Deinococcus radiodurans; the predicted gene product showed significant amino acid sequence homology to several bacterial and eukaryotic SOs, such as the biochemically and structurally characterized enzyme from Arabidopsis thaliana. Cloning of the Deinococcus SO gene was performed by PCR amplification from the bacterial genomic DNA, and heterologous gene expression of a histidine-tagged polypeptide was obtained in a molybdopterin-overproducing strain of Escherichia coli. The recombinant protein was purified to homogeneity by nickel chelating affinity chromatography, and its main kinetic and chemical physical parameters were determined. Northern blot and enzyme activity analyses indicated that draSO gene expression is constitutive in D. radiodurans and that there is no increase upon exposure to thiosulfate and/or molybdenum(II).
More Related Videos
Related Concept Videos
Other Unique Bacteria
Anoxygenic Phototrophic Bacteria
Hyperthermophilic Bacteria
Bacterial Phylum Bacteroidota
Gene Regulation in Microbial Communities: Quorum Sensing

