| Literature DB >> 8647250 |
W Schlenzka1, L Shaw, S Kelm, C L Schmidt, E Bill, A X Trautwein, F Lottspeich, R Schauer.
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 CMP-Neu5Ac and a mononuclear iron centre were also identified.Entities:
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Year: 1996 PMID: 8647250 DOI: 10.1016/0014-5793(96)00384-5
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124