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CMP‐ N ‐acetylneuraminic acid hydroxylase: the first cytosolic Rieske iron‐sulphur protein to be described in Eukarya
Author(s) -
Schlenzka Wiebke,
Shaw Lee,
Kelm Soerge,
Schmidt Christian L.,
Bill Eckhard,
Trautwein Alfred X.,
Lottspeich Friedrich,
Schauer Roland
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)00384-5
Subject(s) - chemistry , cytosol , biochemistry , electron paramagnetic resonance , dithionite , enzyme , crystallography , nuclear magnetic resonance , physics
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 b 5 , the substrate CMP‐Neu5Ac and a mononuclear iron centre were also identified.