| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10537671 | Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics | 2012 | 8 Pages |
Abstract
⺠Comparison of two chlorite dismutases of different subunit and oligomeric structure but similar enzymatic activity. ⺠Significant differences in conformational and thermal stability due to different subunit interactions. ⺠Pentameric (canonical) chlorite dismutase exhibits a high thermal stability and enzymatic activity at high temperatures. ⺠Presented thermodynamic data are representative for chlorite dismutases of two distinct phylogenetic lineages.
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Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Stefan Hofbauer, Kira Gysel, Georg Mlynek, Julius Kostan, Andreas Hagmüller, Holger Daims, Paul G. Furtmüller, Kristina DjinoviÄ-Carugo, Christian Obinger,