8YTS
The structure of the cytochrome c546/556 from Thioalkalivibrio paradoxus with unusual UV-Vis spectral features at atomic resolution
Summary for 8YTS
| Entry DOI | 10.2210/pdb8yts/pdb |
| Descriptor | Cytochrome C, HEME C (3 entities in total) |
| Functional Keywords | cytochrome c546/556, monoheme cytochrome, q-bands splitting, room temperature, two conformations of the propianate group, electron transport |
| Biological source | Thioalkalivibrio paradoxus ARh 1 |
| Total number of polymer chains | 2 |
| Total formula weight | 23289.93 |
| Authors | Varfolomeeva, L.A.,Solovieva, A.Y.,Dergousova, N.I.,Boyko, K.M.,Tikhonova, T.V.,Popov, V.O. (deposition date: 2024-03-26, release date: 2024-04-24, Last modification date: 2025-07-30) |
| Primary citation | Varfolomeeva, L.A.,Solovieva, A.Y.,Shipkov, N.S.,Sluchanko, N.N.,Boyko, K.M.,Khrenova, M.G.,Tikhonova, T.V.,Popov, V.O. Relationship between the structure and physicochemical properties of cytochrome c 546/556 from the bacterium Thioalkalivibrio paradoxus ARh1. Biochem.Biophys.Res.Commun., 778:152340-152340, 2025 Cited by PubMed Abstract: An interplay between the structural and physicochemical properties of the monoheme cytochromes of type c has been extensively studied. However new proteins belonging to this diverse family continue to reveal some novel and unique features. Here, we present the 1.15 Å structure of the low-potential cytochrome c from the bacterium Thioalkalivibrio paradoxus ARh1, which exhibits the prominent splitting of the Q bands in UV-visible spectra even at room temperature. The data obtained suggest that two conformations of the propionate 7 of the heme are responsible for the splitting of the Q bands. We propose that the degree of the splitting of the Q bands is correlated with the conformational lability of the heme propionates. PubMed: 40669334DOI: 10.1016/j.bbrc.2025.152340 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.15 Å) |
Structure validation
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