Výsledky vyhledávání - "Jürgen H Nett"

Changes to the length of the flexible linker region of the Rieske protein impair the interaction of ubiquinol with the cytochromebc1complex

Autor: Jürgen H. Nett, Bernard L. Trumpower, Carola Hunte

Publikováno v: European Journal of Biochemistry. 267:5777-5782

Crystal structures of the cytochrome bc1 complex indicate that the catalytic domain of the Rieske iron-sulfur protein, which carries the [2Fe-2S] cluster, is connected to a transmembrane anchor by a flexible linker region. This flexible linker allows

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::549055f9adac3bd3d3a88fb285fcf81b
https://doi.org/10.1046/j.1432-1327.2000.01650.x

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Intermediate Length Rieske Iron-Sulfur Protein Is Present and Functionally Active in the Cytochrome bc 1Complex of Saccharomyces cerevisiae

Autor: Jürgen H. Nett, Bernard L. Trumpower

Publikováno v: Journal of Biological Chemistry. 274:9253-9257

To investigate the relationship between post-translational processing of the Rieske iron-sulfur protein ofSaccharomyces cerevisiae and its assembly into the mitochondrial cytochrome bc 1 complex we used iron-sulfur proteins in which the presequences

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0e1fffb9321334ccc218ac2a961613c9
https://doi.org/10.1074/jbc.274.14.9253

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Two-step Processing Is Not Essential for the Import and Assembly of Functionally Active Iron-Sulfur Protein into the Cytochrome bc1 Complex in Saccharomyces cerevisiae

Autor: Jürgen H. Nett, Bernard L. Trumpower, Elke Denke

Publikováno v: Journal of Biological Chemistry. 272:2212-2217

The iron-sulfur protein of the cytochrome bc1 complex is one of a small number of proteins that are processed in two sequential steps by matrix processing peptidase (MPP) and mitochondrial intermediate peptidase (MIP) during import into Saccharomyces

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::142b6076284ae7eb91b3a8a0c02af9f6
https://doi.org/10.1074/jbc.272.4.2212

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Dissociation of Import of the Rieske Iron-Sulfur Protein into Saccharomyces cerevisiae Mitochondria from Proteolytic Processing of the Presequence

Autor: Bernard L. Trumpower, Jürgen H. Nett

Publikováno v: Journal of Biological Chemistry. 271:26713-26716

The correlation between the import of the Rieske iron-sulfur protein into the mitochondrial matrix and processing of the precursor protein by matrix processing peptidase was investigated using high concentrations of metal chelators and iron-sulfur pr

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::152e2c294bca132241480f3829b64bb9
https://doi.org/10.1074/jbc.271.43.26713

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Investigating the structure of nucleotide binding sites on the chloroplast F1-ATPase using electron spin resonance spectroscopy

Autor: Guy Girault, Ralf M. Lösel, John G. Wise, Pia D. Vogel, Gerard Berger, Annette H Erbse, Jürgen H Nett

Publikováno v: Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy. 52:73-83

The relative structure and binding properties of nucleotide binding sites of the latent, nonactivated chloroplast F1(CF1)ATPase have been investigated by employing ESR spectroscopy using 2-N3-2′,3′-SL-ATP (2-N3-SL-ATP), a spin-labeled photoaffini

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::7ce337bb9feafd088248ab7ef865df98
https://doi.org/10.1016/0584-8539(95)01549-3

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The interaction of atovaquone with the P. carinii cytochrome bc1 complex

Autor: Steven R. Meshnick, Bernard L. Trumpower, Powel Kazanjian, Edward A. Berry, Jürgen H. Nett

Publikováno v: The Journal of eukaryotic microbiology.

Author(s): Trumpower, B. | Abstract: Atovaquone is an important second-line therapeutic and prophylactic agent for Pneumocystis carinii pneumonia although it was originally developed as an antimalarial [11]. For malaria, atovaquone is now only used i

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::415705879dd8cfb22b6717e8754ca009
https://pubmed.ncbi.nlm.nih.gov/11906048

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Processing of the presequence of the Schizosaccharomyces pombe Rieske iron-sulfur protein occurs in a single step and can be converted to two-step processing by mutation of a single proline to serine in the presequence

Autor: Jürgen H. Nett, Bernard L. Trumpower, Hermann Schägger

Publikováno v: The Journal of biological chemistry. 273(15)

The iron-sulfur proteins of the cytochrome bc1 complexes of Schizosaccharomyces pombe and Saccharomyces cerevisiae contain the three amino acid motif RX( downward arrow)(F/L/I)XX(T/S/G)XXXX (downward arrow) that is typical for proteins that are cleav

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a9a4383361a289225d92beff23a0334e
https://pubmed.ncbi.nlm.nih.gov/9535840

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The cleaved presequence is not required for import of subunit 6 of the cytochrome bc1 complex into yeast mitochondria or assembly into the complex*

Autor: Marie Laure DeLabre, Bernard L. Trumpower, Jürgen H. Nett

Publikováno v: FEBS Letters. (2-3):201-205

Subunit 6 of the yeast cytochrome bc1 complex contains a 25 amino acid presequence that is not present in the mature form of the protein in the bc1 complex. The presequence of subunit 6 is atypical of presequences responsible for targeting proteins t

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