Sulfite-oxidizing enzymes

  • Ulrike KapplerEmail author
  • John H. Enemark
Part of the following topical collections:
  1. Topical Issue on Molybdenum and Tungsten Enzymes: from Biology to Chemistry and Back


Sulfite-oxidizing enzymes (SOEs) are molybdenum enzymes that exist in almost all forms of life where they carry out important functions in protecting cells and organisms against sulfite-induced damage. Due to their nearly ubiquitous presence in living cells, these enzymes can be assumed to be evolutionarily ancient, and this is reflected in the fact that the basic domain architecture and fold structure of all sulfite-oxidizing enzymes studied so far are similar. The Mo centers of all SOEs have five-coordinate square pyramidal coordination geometry, which incorporates a pyranopterin dithiolene cofactor. However, significant differences exist in the quaternary structure of the enzymes, as well as in the kinetic properties and the nature of the electron acceptors used. In addition, some SOEs also contain an integral heme group that participates in the overall catalytic cycle. Catalytic turnover involves the paramagnetic Mo(V) oxidation state, and EPR spectroscopy, especially high-resolution pulsed EPR spectroscopy, provides detailed information about the molecular and electronic structure of the Mo center and the Mo-based sulfite oxidation reaction.


Sulfite oxidation Electron transfer Electron paramagnetic resonance Molybdenum enzyme Pyranopterin dithiolene 



Chicken sulfite oxidase


Continuous wave electron paramagnetic resonance

Cyt c

Cytochrome c


Density functional theory


Electron spin echo


Electron spin echo envelope modulation


Human sulfite oxidase


Intramolecular electron transfer


Pyranopterin dithiolene


Plant sulfite oxidase


Sulfite dehydrogenase


Sulfite oxidase


Sulfite-oxidizing enzyme


SorAB sulfite dehydrogenase from Starkeya novella


SorT sulfite dehydrogenase from Sinorhizobium meliloti


c-type cytochrome, natural electron acceptor for SorT


Sulfite oxidase



JHE gratefully acknowledges many years of financial support from NIGMS for research on molybdenum enzymes (Grant GM-037773). We thank A. Belaidi and G. Schwarz for a preprint of Ref. [54] and Dr. Megan Maher for help with the preparation of Figs. 1 and 3 and for a preprint of Ref. [40].

Supplementary material

775_2014_1197_MOESM1_ESM.pdf (73 kb)
Supplementary material 1 (PDF 72 kb)


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Copyright information

© SBIC 2014

Authors and Affiliations

  1. 1.Centre for Metals in Biology, School of Chemistry and Molecular BiosciencesThe University of QueenslandSt. LuciaAustralia
  2. 2.Department of Chemistry and BiochemistryUniversity of ArizonaTucsonUSA

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