Abstract
Electron paramagnetic resonance (EPR) spectroscopy and analysis of the primary structure of the CMP-N-acetylneuraminic acid hydroxylase revealed that this enzyme is the first iron-sulphur protein of the Rieske type to be found in the cytosol of Eukarya. The dithionite-reduced hydroxylase exhibited an EPR signal known to be characteristic for a Rieske iron-sulphur centre (2Fe-2S), the g-values being 1.78, 1.91 and 2.01, respectively. An analysis of the primary structure of the hydroxylase led to the identification of an amino acid sequence, known to be characteristic for Rieske proteins. Furthermore, possible binding sites for cytochrome b5, the substrate CMPNeu5Ac and a mononuclear iron centre were also identified.
| Original language | English |
|---|---|
| Journal | FEBS Letters |
| Volume | 385 |
| Issue number | 3 |
| Pages (from-to) | 197-200 |
| Number of pages | 4 |
| ISSN | 0014-5793 |
| DOIs | |
| Publication status | Published - 06.05.1996 |
Funding
Acknowledgements: The financial support of the Fonds der Che-mischen lndustrie, the Deutsche Forschungsgemeinschaft (Grant No. Scha 202/20-1), the Mizutani Foundation (Grant No. 145b) and the Sialic Acids Society (Kiel) is gratefully acknowledged.