Purification and characterization of the Rieske iron-sulfur protein from the thermoacidophilic crenarchaeon Sulfolobus acidocaldarius

C. L. Schmidt; S. Anemüller; M. Teixeira; G. Schäfer

doi:10.1016/0014-5793(94)00052-W

Purification and characterization of the Rieske iron-sulfur protein from the thermoacidophilic crenarchaeon Sulfolobus acidocaldarius

C. L. Schmidt, S. Anemüller, M. Teixeira, G. Schäfer^*

^*Corresponding author for this work

Institute of Biochemistry

Instituto de Tecnologia Quimica e Biologica - Univesidade Nova de Lisboa

24 Citations (Scopus)

Abstract

The previously detected Rieske iron-sulfur protein from the membranes of the thermoacidophile Sulfolobus acidocaldarius [Anemüller, S., et al. (1993) FEBS Lett. 318, 61-64] was purified to electrophoretic homogeneity and the N-terminal amino acids determined. The apparent molecular weight was estimated to be 32 kDa. The reduced protein displays a rhombic EPR spectrum with g_xyz = 1.768, 1.895, 2.035. The average g-value of 1.902 is typical for nitrogen ligand-containing clusters. EPR spin quantification and the iron content indicate the presence of one [2Fe-2S] cluster. The purified protein displaus ubiquinol cytochrome c reductase activity. The pH optimum of this reaction is temperature dependent and was determined to be pH 7 at 56°C. The results presented in this study clearly prove that the Sulfolobus Rieske protein belongs to the family of the true Rieske iron-sulfur proteins.

Original language	English
Journal	FEBS Letters
Volume	359
Issue number	2-3
Pages (from-to)	239-243
Number of pages	5
ISSN	0014-5793
DOIs	https://doi.org/10.1016/0014-5793(94)00052-W
Publication status	Published - 13.02.1995

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Academic Focus: Center for Infection and Inflammation Research (ZIEL)

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10.1016/0014-5793(94)00052-W

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@article{f8442313e26f4e99ba404272fc07b2fb,

title = "Purification and characterization of the Rieske iron-sulfur protein from the thermoacidophilic crenarchaeon Sulfolobus acidocaldarius",

abstract = "The previously detected Rieske iron-sulfur protein from the membranes of the thermoacidophile Sulfolobus acidocaldarius [Anem{\"u}ller, S., et al. (1993) FEBS Lett. 318, 61-64] was purified to electrophoretic homogeneity and the N-terminal amino acids determined. The apparent molecular weight was estimated to be 32 kDa. The reduced protein displays a rhombic EPR spectrum with gxyz = 1.768, 1.895, 2.035. The average g-value of 1.902 is typical for nitrogen ligand-containing clusters. EPR spin quantification and the iron content indicate the presence of one [2Fe-2S] cluster. The purified protein displaus ubiquinol cytochrome c reductase activity. The pH optimum of this reaction is temperature dependent and was determined to be pH 7 at 56°C. The results presented in this study clearly prove that the Sulfolobus Rieske protein belongs to the family of the true Rieske iron-sulfur proteins.",

author = "Schmidt, {C. L.} and S. Anem{\"u}ller and M. Teixeira and G. Sch{\"a}fer",

note = "Funding Information: Acknowledgements: The authors wish to thank E. Bill for his kind help with the EPR spectroscopy in Lfibeck, R. Schmid for the N-terminal sequence analysis, and Prof. M. Brunori for providing cytochrome c55~ from Pseudomonas aeruginosa. This work was supported by a grant from the European community (EEC project BIO2-CT93-0274), JNICT, Portugal (Grant STRDAdC/BIOI416/92 to M.T.) and grants from the Deutsche Forschungsgemeinschaft (DFG) to S.A. and G.S. Copyright: Copyright 2015 Elsevier B.V., All rights reserved.",

year = "1995",

month = feb,

day = "13",

doi = "10.1016/0014-5793(94)00052-W",

language = "English",

volume = "359",

pages = "239--243",

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T1 - Purification and characterization of the Rieske iron-sulfur protein from the thermoacidophilic crenarchaeon Sulfolobus acidocaldarius

AU - Schmidt, C. L.

AU - Anemüller, S.

AU - Teixeira, M.

AU - Schäfer, G.

N1 - Funding Information: Acknowledgements: The authors wish to thank E. Bill for his kind help with the EPR spectroscopy in Lfibeck, R. Schmid for the N-terminal sequence analysis, and Prof. M. Brunori for providing cytochrome c55~ from Pseudomonas aeruginosa. This work was supported by a grant from the European community (EEC project BIO2-CT93-0274), JNICT, Portugal (Grant STRDAdC/BIOI416/92 to M.T.) and grants from the Deutsche Forschungsgemeinschaft (DFG) to S.A. and G.S. Copyright: Copyright 2015 Elsevier B.V., All rights reserved.

PY - 1995/2/13

Y1 - 1995/2/13

N2 - The previously detected Rieske iron-sulfur protein from the membranes of the thermoacidophile Sulfolobus acidocaldarius [Anemüller, S., et al. (1993) FEBS Lett. 318, 61-64] was purified to electrophoretic homogeneity and the N-terminal amino acids determined. The apparent molecular weight was estimated to be 32 kDa. The reduced protein displays a rhombic EPR spectrum with gxyz = 1.768, 1.895, 2.035. The average g-value of 1.902 is typical for nitrogen ligand-containing clusters. EPR spin quantification and the iron content indicate the presence of one [2Fe-2S] cluster. The purified protein displaus ubiquinol cytochrome c reductase activity. The pH optimum of this reaction is temperature dependent and was determined to be pH 7 at 56°C. The results presented in this study clearly prove that the Sulfolobus Rieske protein belongs to the family of the true Rieske iron-sulfur proteins.

AB - The previously detected Rieske iron-sulfur protein from the membranes of the thermoacidophile Sulfolobus acidocaldarius [Anemüller, S., et al. (1993) FEBS Lett. 318, 61-64] was purified to electrophoretic homogeneity and the N-terminal amino acids determined. The apparent molecular weight was estimated to be 32 kDa. The reduced protein displays a rhombic EPR spectrum with gxyz = 1.768, 1.895, 2.035. The average g-value of 1.902 is typical for nitrogen ligand-containing clusters. EPR spin quantification and the iron content indicate the presence of one [2Fe-2S] cluster. The purified protein displaus ubiquinol cytochrome c reductase activity. The pH optimum of this reaction is temperature dependent and was determined to be pH 7 at 56°C. The results presented in this study clearly prove that the Sulfolobus Rieske protein belongs to the family of the true Rieske iron-sulfur proteins.

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Purification and characterization of the Rieske iron-sulfur protein from the thermoacidophilic crenarchaeon Sulfolobus acidocaldarius

Abstract

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