Výsledky vyhledávání - "Michela, Castellani"

X-ray structure of the dimeric cytochrome bc1 complex from the soil bacterium Paracoccus denitrificans at 2.7-Å resolution

Autor: Michela Castellani, Nina Morgner, Chi H. Trinh, Thomas Kleinschroth, Carola Hunte, Bernhard Brutschy, Bernd Ludwig

Publikováno v: Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1807:1606-1615

The respiratory cytochrome bc(1) complex is a fundamental enzyme in biological energy conversion. It couples electron transfer from ubiquinol to cytochrome c with generation of proton motive force which fuels ATP synthesis. The complex from the α-pr

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6bb3f3d95e90f92f88a1c971a62308ed
https://doi.org/10.1016/j.bbabio.2011.09.017

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Direct Demonstration of Half-of-the-sites Reactivity in the Dimeric Cytochrome bc1 Complex

Autor: Bernard L. Trumpower, Michela Castellani, Oliver Anderka, Bernd Ludwig, Thomas Kleinschroth, Raul Covian

Publikováno v: Journal of Biological Chemistry. 285:502-510

We previously proposed that the dimeric cytochrome bc1 complex exhibits half-of-the-sites reactivity for ubiquinol oxidation and rapid electron transfer between bc1 monomers (Covian, R., Kleinschroth, T., Ludwig, B., and Trumpower, B. L. (2007) J. Bi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::22eb1d8aeb858065f2d6ed8691577e5b
https://doi.org/10.1074/jbc.m109.072959

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Photoinitiated electron transfer within the Paracoccus denitrificans cytochrome bc1 complex: mobility of the iron-sulfur protein is modulated by the occupant of the Q(o) site

Autor: Thomas Kleinschroth, Bernd Ludwig, Francis Millett, Michela Castellani, Jeffrey Havens, Bill Durham

Publikováno v: Biochemistry. 50(48)

Domain rotation of the Rieske iron-sulfur protein (ISP) between the cytochrome (cyt) b and cyt c(1) redox centers plays a key role in the mechanism of the cyt bc(1) complex. Electron transfer within the cyt bc(1) complex of Paracoccus denitrificans w

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8de408e20c570e573b76e2c62c70c797
https://pubmed.ncbi.nlm.nih.gov/22026826

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Direct demonstration of half-of-the-sites reactivity in the dimeric cytochrome bc1 complex: enzyme with one inactive monomer is fully active but unable to activate the second ubiquinol oxidation site in response to ligand binding at the ubiquinone reduction site

Autor: Michela, Castellani, Raul, Covian, Thomas, Kleinschroth, Oliver, Anderka, Bernd, Ludwig, Bernard L, Trumpower

Publikováno v: The Journal of biological chemistry. 285(1)

We previously proposed that the dimeric cytochrome bc(1) complex exhibits half-of-the-sites reactivity for ubiquinol oxidation and rapid electron transfer between bc(1) monomers (Covian, R., Kleinschroth, T., Ludwig, B., and Trumpower, B. L. (2007) J

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::d59deee4532ec476b33537822b438ff2
https://pubmed.ncbi.nlm.nih.gov/19892700

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Heterodimeric bc1 complex from Paracoccus denitrificans: A validation of the half-of-the-sites mechanism

Autor: Bernard L. Trumpower, Thomas Kleinschroth, Raul Covian, Bernd Ludwig, Michela Castellani

Publikováno v: Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1797:112-113

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::520b4fd6358662ffe2fad2396460e171
https://doi.org/10.1016/j.bbabio.2010.04.338

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The acidic domain of cytochrome c1 in Paracoccus denitrificans, analogous to the acidic subunits in eukaryotic bc1 complexes, is not involved in the electron transfer reaction to its native substrate cytochrome c552

Autor: Francis Millett, Bernd Ludwig, Francesco Malatesta, Thomas Kleinschroth, Michela Castellani, Jeffrey Havens, Bill Durham

Publikováno v: Biochimica et Biophysica Acta (BBA) - Bioenergetics. (11):1383-1389

The cytochrome bc1 complex is a key component in several respiratory pathways. One of the characteristics of the eukaryotic complex is the presence of a small acidic subunit, which is thought to guide the interaction of the complex with its electron

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