CMP‐N‐acetylneuraminic acid hydroxylase: the first cytosolic Rieske iron‐sulphur protein to be described in Eukarya

FEBS Letters

Schmidt, Christian L.¹  Lottspeich, Friedrich²  Schauer, Roland³  Kelm, Soerge³  Bill, Eckhard⁴  Schlenzka, Wiebke³  Trautwein, Alfred X.⁴  Shaw, Lee³ 

[1] Institut für Biochemie der Medizinischen Universität Lübeck, Ratzeburger Allee 160, 23538 Lübeck, Germany;Max-Planck-Institut für Biochemie, Am Klopferspitz 18a, 82152 Martinsried, Germany;Biochemisches Institut der Christian-Albrechts-Universität zu Kiel, Olshausenstr. 40, 24098 Kiel, Germany;Institut für Physik der Medizinischen Universität Lübeck, Ratzeburger Allee 160, 23538 Lübeck, Germany

关键词: Hydroxylase;    Rieske protein;    Sialic acid;    Electron paramagnetic resonance;    CMP-N-acetylneuraminic acid;    N-Glycolylneuraminic acid;   

DOI  :  10.1016/0014-5793(96)00384-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown