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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Schlenzka W,Shaw L,Kelm S,Schmidt CL,Bill E,Trautwein AX,Lottspeich F,Schauer Rdoi
10.1016/0014-5793(96)00384-5subject
Has Abstractpub_date
1996-05-06 00:00:00pages
197-200issue
3eissn
0014-5793issn
1873-3468pii
0014-5793(96)00384-5journal_volume
385pub_type
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