Sulfite-oxidizing enzymes

Kappler, Ulrike and Enemark, John H. (2014) Sulfite-oxidizing enzymes. Journal of Biological Inorganic Chemistry, 20 2: 253-264. doi:10.1007/s00775-014-1197-3

Author Kappler, Ulrike
Enemark, John H.
Title Sulfite-oxidizing enzymes
Journal name Journal of Biological Inorganic Chemistry   Check publisher's open access policy
ISSN 0949-8257
Publication date 2014-09
Year available 2014
Sub-type Article (original research)
DOI 10.1007/s00775-014-1197-3
Open Access Status
Volume 20
Issue 2
Start page 253
End page 264
Total pages 12
Place of publication Heidelberg, Germany
Publisher Springer
Collection year 2015
Language eng
Abstract 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.
Keyword Electron paramagnetic resonance
Electron transfer
Molybdenum enzyme
Pyranopterin dithiolene
Sulfite oxidation
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ
Additional Notes Published online: 27 September 2014.

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2015 Collection
School of Chemistry and Molecular Biosciences
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Created: Fri, 03 Oct 2014, 11:55:32 EST by Mrs Louise Nimwegen on behalf of School of Chemistry & Molecular Biosciences