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

Wiebke Schlenzka, Lee Shaw, Soerge Kelm, Christian L. Schmidt, Eckhard Bill, Alfred X. Trautwein, Friedrich Lottspeich, Roland Schauer*

*Corresponding author for this work
59 Citations (Scopus)

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 languageEnglish
JournalFEBS Letters
Volume385
Issue number3
Pages (from-to)197-200
Number of pages4
ISSN0014-5793
DOIs
Publication statusPublished - 06.05.1996

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