caa a22 4500 605507910 CHVBK 20210128100634.0 cr unu---uuuuu 210128e20150301xx s 000 0 eng 10.1007/s00775-014-1197-3 doi (NATIONALLICENCE)springer-10.1007/s00775-014-1197-3 Sulfite-oxidizing enzymes [Elektronische Daten] [Ulrike Kappler, John Enemark] 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. SBIC, 2014 Sulfite oxidation nationallicence Electron transfer nationallicence Electron paramagnetic resonance nationallicence Molybdenum enzyme nationallicence Pyranopterin dithiolene nationallicence CSO : Chicken sulfite oxidase nationallicence CW EPR : Continuous wave electron paramagnetic resonance nationallicence Cyt c : Cytochrome c nationallicence DFT : Density functional theory nationallicence ESE : Electron spin echo nationallicence ESEEM : Electron spin echo envelope modulation nationallicence HSO : Human sulfite oxidase nationallicence IET : Intramolecular electron transfer nationallicence PPT : Pyranopterin dithiolene nationallicence PSO : Plant sulfite oxidase nationallicence SDH : Sulfite dehydrogenase nationallicence SO : Sulfite oxidase nationallicence SOE : Sulfite-oxidizing enzyme nationallicence SorAB : SorAB sulfite dehydrogenase from Starkeya novella nationallicence SorT : SorT sulfite dehydrogenase from Sinorhizobium meliloti nationallicence SorU : c-type cytochrome, natural electron acceptor for SorT nationallicence SUOX : Sulfite oxidase nationallicence Kappler Ulrike Centre for Metals in Biology, School of Chemistry and Molecular Biosciences, The University of Queensland, 4072, St. Lucia, QLD, Australia aut Enemark John Department of Chemistry and Biochemistry, University of Arizona, 85721-0041, Tucson, AZ, USA aut JBIC Journal of Biological Inorganic Chemistry Springer Berlin Heidelberg 20/2(2015-03-01), 253-264 0949-8257 20:2<253 2015 20 775 https://doi.org/10.1007/s00775-014-1197-3 text/html Onlinezugriff via DOI BK010053 XK010053 XK010000 Metadata rights reserved Springer special CC-BY-NC licence nationallicence 1 review-article jats NATIONALLICENCE NATIONALLICENCE NL-springer NATIONALLICENCE 856 40 https://doi.org/10.1007/s00775-014-1197-3 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Kappler Ulrike Centre for Metals in Biology, School of Chemistry and Molecular Biosciences, The University of Queensland, 4072, St. Lucia, QLD, Australia aut NATIONALLICENCE 700 1- Enemark John Department of Chemistry and Biochemistry, University of Arizona, 85721-0041, Tucson, AZ, USA aut NATIONALLICENCE 773 0- JBIC Journal of Biological Inorganic Chemistry Springer Berlin Heidelberg 20/2(2015-03-01), 253-264 0949-8257 20:2<253 2015 20 775