Unanswered questions about the structure of cytochrome bc1 complexes
| Autor: | Heather De Bari, Li-Shar Huang, Edward A. Berry |
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| Rok vydání: | 2013 |
| Předmět: |
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Molecular Hemeprotein Cytochrome Stereochemistry Protein Conformation Complex III Molecular Sequence Data Biophysics Heme Biochemistry chemistry.chemical_compound Electron Transport Complex III Protein structure Non-pro cis peptide Animals Humans Ubiquinol:cytochrome c reductase Amino Acid Sequence Heme orientation Heme protein biology Sequence Homology Amino Acid Chemistry Cytochrome bc1 Matrix processing peptidase Cell Biology Rieske iron-sulfur protein Transmembrane domain Heme B Crystallography Protein Subunits Coenzyme Q – cytochrome c reductase biology.protein |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1827(11-12):1258-1277 |
| ISSN: | 0005-2728 |
| DOI: | 10.1016/j.bbabio.2013.04.006 |
| Popis: | X-ray crystal structures of bc1 complexes obtained over the last 15 years have provided a firm structural basis for our understanding of the complex. For the most part there is good agreement between structures from different species, different crystal forms, and with different inhibitors bound. In this review we focus on some of the remaining unexplained differences, either between the structures themselves or the interpretations of the structural observations. These include the structural basis for the motion of the Rieske iron–sulfur protein in response to inhibitors, a possible conformational change involving tyrosine132 of cytochrome (cyt) b, the presence of cis-peptides at the beginnings of transmembrane helices C, E, and H, the structural insight into the function of the so-called “Core proteins”, different modelings of the retained signal peptide, orientation of the low-potential heme b, and chirality of the Met ligand to heme c1. This article is part of a Special Issue entitled: Respiratory complex III and related bc complexes. |
| Databáze: | OpenAIRE |
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