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

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 Lett

journal_title

FEBS letters

authors

Schlenzka W,Shaw L,Kelm S,Schmidt CL,Bill E,Trautwein AX,Lottspeich F,Schauer R

doi

10.1016/0014-5793(96)00384-5

subject

Has Abstract

pub_date

1996-05-06 00:00:00

pages

197-200

issue

3

eissn

0014-5793

issn

1873-3468

pii

0014-5793(96)00384-5

journal_volume

385

pub_type

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