Sulfite-oxidizing enzymes
| LEADER | caa a22 4500 | ||
|---|---|---|---|
| 001 | 605507910 | ||
| 003 | CHVBK | ||
| 005 | 20210128100634.0 | ||
| 007 | cr unu---uuuuu | ||
| 008 | 210128e20150301xx s 000 0 eng | ||
| 024 | 7 | 0 | |a 10.1007/s00775-014-1197-3 |2 doi |
| 035 | |a (NATIONALLICENCE)springer-10.1007/s00775-014-1197-3 | ||
| 245 | 0 | 0 | |a Sulfite-oxidizing enzymes |h [Elektronische Daten] |c [Ulrike Kappler, John Enemark] |
| 520 | 3 | |a 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. | |
| 540 | |a SBIC, 2014 | ||
| 690 | 7 | |a Sulfite oxidation |2 nationallicence | |
| 690 | 7 | |a Electron transfer |2 nationallicence | |
| 690 | 7 | |a Electron paramagnetic resonance |2 nationallicence | |
| 690 | 7 | |a Molybdenum enzyme |2 nationallicence | |
| 690 | 7 | |a Pyranopterin dithiolene |2 nationallicence | |
| 690 | 7 | |a CSO : Chicken sulfite oxidase |2 nationallicence | |
| 690 | 7 | |a CW EPR : Continuous wave electron paramagnetic resonance |2 nationallicence | |
| 690 | 7 | |a Cyt c : Cytochrome c |2 nationallicence | |
| 690 | 7 | |a DFT : Density functional theory |2 nationallicence | |
| 690 | 7 | |a ESE : Electron spin echo |2 nationallicence | |
| 690 | 7 | |a ESEEM : Electron spin echo envelope modulation |2 nationallicence | |
| 690 | 7 | |a HSO : Human sulfite oxidase |2 nationallicence | |
| 690 | 7 | |a IET : Intramolecular electron transfer |2 nationallicence | |
| 690 | 7 | |a PPT : Pyranopterin dithiolene |2 nationallicence | |
| 690 | 7 | |a PSO : Plant sulfite oxidase |2 nationallicence | |
| 690 | 7 | |a SDH : Sulfite dehydrogenase |2 nationallicence | |
| 690 | 7 | |a SO : Sulfite oxidase |2 nationallicence | |
| 690 | 7 | |a SOE : Sulfite-oxidizing enzyme |2 nationallicence | |
| 690 | 7 | |a SorAB : SorAB sulfite dehydrogenase from Starkeya novella |2 nationallicence | |
| 690 | 7 | |a SorT : SorT sulfite dehydrogenase from Sinorhizobium meliloti |2 nationallicence | |
| 690 | 7 | |a SorU : c-type cytochrome, natural electron acceptor for SorT |2 nationallicence | |
| 690 | 7 | |a SUOX : Sulfite oxidase |2 nationallicence | |
| 700 | 1 | |a Kappler |D Ulrike |u Centre for Metals in Biology, School of Chemistry and Molecular Biosciences, The University of Queensland, 4072, St. Lucia, QLD, Australia |4 aut | |
| 700 | 1 | |a Enemark |D John |u Department of Chemistry and Biochemistry, University of Arizona, 85721-0041, Tucson, AZ, USA |4 aut | |
| 773 | 0 | |t JBIC Journal of Biological Inorganic Chemistry |d Springer Berlin Heidelberg |g 20/2(2015-03-01), 253-264 |x 0949-8257 |q 20:2<253 |1 2015 |2 20 |o 775 | |
| 856 | 4 | 0 | |u https://doi.org/10.1007/s00775-014-1197-3 |q text/html |z Onlinezugriff via DOI |
| 898 | |a BK010053 |b XK010053 |c XK010000 | ||
| 900 | 7 | |a Metadata rights reserved |b Springer special CC-BY-NC licence |2 nationallicence | |
| 908 | |D 1 |a review-article |2 jats | ||
| 949 | |B NATIONALLICENCE |F NATIONALLICENCE |b NL-springer | ||
| 950 | |B NATIONALLICENCE |P 856 |E 40 |u https://doi.org/10.1007/s00775-014-1197-3 |q text/html |z Onlinezugriff via DOI | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Kappler |D Ulrike |u Centre for Metals in Biology, School of Chemistry and Molecular Biosciences, The University of Queensland, 4072, St. Lucia, QLD, Australia |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Enemark |D John |u Department of Chemistry and Biochemistry, University of Arizona, 85721-0041, Tucson, AZ, USA |4 aut | ||
| 950 | |B NATIONALLICENCE |P 773 |E 0- |t JBIC Journal of Biological Inorganic Chemistry |d Springer Berlin Heidelberg |g 20/2(2015-03-01), 253-264 |x 0949-8257 |q 20:2<253 |1 2015 |2 20 |o 775 | ||