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

doi:10.1016/0014-5793(96)00384-5

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^*

^*Korrespondierende/r Autor/-in für diese Arbeit

73 Zitate (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.

Originalsprache	Englisch
Zeitschrift	FEBS Letters
Jahrgang	385
Ausgabenummer	3
Seiten (von - bis)	197-200
Seitenumfang	4
ISSN	0014-5793
DOIs	https://doi.org/10.1016/0014-5793(96)00384-5
Publikationsstatus	Veröffentlicht - 06.05.1996

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Acknowledgements: The financial support of the Fonds der Che-mischen lndustrie, the Deutsche Forschungsgemeinschaft (Grant No. Scha 202/20-1), the Mizutani Foundation (Grant No. 145b) and the Sialic Acids Society (Kiel) is gratefully acknowledged.

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title = "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 CMPNeu5Ac and a mononuclear iron centre were also identified.",

author = "Wiebke Schlenzka and Lee Shaw and Soerge Kelm and Schmidt, \{Christian L.\} and Eckhard Bill and Trautwein, \{Alfred X.\} and Friedrich Lottspeich and Roland Schauer",

year = "1996",

month = may,

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doi = "10.1016/0014-5793(96)00384-5",

language = "English",

volume = "385",

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journal = "FEBS Letters",

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T1 - CMP-N-acetylneuraminic acid hydroxylase: The first cytosolic Rieske iron-sulphur protein to be described in Eukarya

AU - Schlenzka, Wiebke

AU - Shaw, Lee

AU - Kelm, Soerge

AU - Schmidt, Christian L.

AU - Bill, Eckhard

AU - Trautwein, Alfred X.

AU - Lottspeich, Friedrich

AU - Schauer, Roland

PY - 1996/5/6

Y1 - 1996/5/6

N2 - 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.

AB - 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.

UR - https://www.scopus.com/pages/publications/0029941677

U2 - 10.1016/0014-5793(96)00384-5

DO - 10.1016/0014-5793(96)00384-5

M3 - Journal articles

C2 - 8647250

AN - SCOPUS:0029941677

SN - 0014-5793

VL - 385

SP - 197

EP - 200

JO - FEBS Letters

JF - FEBS Letters

IS - 3

ER -

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

Abstract

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