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Journal Abstract Search
733 related items for PubMed ID: 9609705
1. Interactions between the cytochrome b, cytochrome c1, and Fe-S protein subunits at the ubihydroquinone oxidation site of the bc1 complex of Rhodobacter capsulatus. Saribaş AS, Valkova-Valchanova M, Tokito MK, Zhang Z, Berry EA, Daldal F. Biochemistry; 1998 Jun 02; 37(22):8105-14. PubMed ID: 9609705 [Abstract] [Full Text] [Related]
2. Isolation and characterization of a two-subunit cytochrome b-c1 subcomplex from Rhodobacter capsulatus and reconstitution of its ubihydroquinone oxidation (Qo) site with purified Fe-S protein subunit. Valkova-Valchanova MB, Saribas AS, Gibney BR, Dutton PL, Daldal F. Biochemistry; 1998 Nov 17; 37(46):16242-51. PubMed ID: 9819216 [Abstract] [Full Text] [Related]
3. The amino-terminal portion of the Rieske iron-sulfur protein contributes to the ubihydroquinone oxidation site catalysis of the Rhodobacter capsulatus bc1 complex. Brasseur G, Sled V, Liebl U, Ohnishi T, Daldal F. Biochemistry; 1997 Sep 30; 36(39):11685-96. PubMed ID: 9305958 [Abstract] [Full Text] [Related]
4. Protein-protein interactions between cytochrome b and the Fe-S protein subunits during QH2 oxidation and large-scale domain movement in the bc1 complex. Darrouzet E, Daldal F. Biochemistry; 2003 Feb 18; 42(6):1499-507. PubMed ID: 12578362 [Abstract] [Full Text] [Related]
5. The cytochrome b Zn binding amino acid residue histidine 291 is essential for ubihydroquinone oxidation at the Qo site of bacterial cytochrome bc1. Francia F, Malferrari M, Lanciano P, Steimle S, Daldal F, Venturoli G. Biochim Biophys Acta; 2016 Nov 18; 1857(11):1796-1806. PubMed ID: 27550309 [Abstract] [Full Text] [Related]
6. Substitution of the sixth axial ligand of Rhodobacter capsulatus cytochrome c1 heme yields novel cytochrome c1 variants with unusual properties. Darrouzet E, Mandaci S, Li J, Qin H, Knaff DB, Daldal F. Biochemistry; 1999 Jun 22; 38(25):7908-17. PubMed ID: 10387032 [Abstract] [Full Text] [Related]
7. Tyrosine 147 of cytochrome b is required for efficient electron transfer at the ubihydroquinone oxidase site (Qo) of the cytochrome bc1 complex. Saribaş AS, Ding H, Dutton PL, Daldal F. Biochemistry; 1995 Dec 12; 34(49):16004-12. PubMed ID: 8519756 [Abstract] [Full Text] [Related]
8. Substitutions at position 146 of cytochrome b affect drastically the properties of heme bL and the Qo site of Rhodobacter capsulatus cytochrome bc1 complex. Saribaş AS, Ding H, Dutton PL, Daldal F. Biochim Biophys Acta; 1997 Mar 28; 1319(1):99-108. PubMed ID: 9107318 [Abstract] [Full Text] [Related]
9. The cytochrome b lysine 329 residue is critical for ubihydroquinone oxidation and proton release at the Qo site of bacterial cytochrome bc1. Francia F, Khalfaoui-Hassani B, Lanciano P, Musiani F, Noodleman L, Venturoli G, Daldal F. Biochim Biophys Acta Bioenerg; 2019 Feb 01; 1860(2):167-179. PubMed ID: 30550726 [Abstract] [Full Text] [Related]
10. Cytochrome bc1 complex [2Fe-2S] cluster and its interaction with ubiquinone and ubihydroquinone at the Qo site: a double-occupancy Qo site model. Ding H, Robertson DE, Daldal F, Dutton PL. Biochemistry; 1992 Mar 31; 31(12):3144-58. PubMed ID: 1313287 [Abstract] [Full Text] [Related]
11. A structural model for across membrane coupling between the Qo and Qi active sites of cytochrome bc1. Cooley JW. Biochim Biophys Acta; 2010 Dec 31; 1797(12):1842-8. PubMed ID: 20513347 [Abstract] [Full Text] [Related]
12. Ion pair formation between basic residues at 144 of the Cyt b polypeptide and the ubiquinones at the Qo site of the Cyt bc1 complex. Ding H, Daldal F, Dutton PL. Biochemistry; 1995 Dec 12; 34(49):15997-6003. PubMed ID: 8519755 [Abstract] [Full Text] [Related]
13. Functional flexibility of electron flow between quinol oxidation Qo site of cytochrome bc1 and cytochrome c revealed by combinatory effects of mutations in cytochrome b, iron-sulfur protein and cytochrome c1. Borek A, Ekiert R, Osyczka A. Biochim Biophys Acta Bioenerg; 2018 Sep 12; 1859(9):754-761. PubMed ID: 29705394 [Abstract] [Full Text] [Related]
14. Roles in inhibitor recognition and quinol oxidation of the amino acid side chains at positions of cyt b providing resistance to Qo-inhibitors of the bc1 complex from Rhodobacter capsulatus. Tokito MK, Daldal F. Mol Microbiol; 1993 Sep 12; 9(5):965-78. PubMed ID: 7934923 [Abstract] [Full Text] [Related]