8AJZ
Serial femtosecond crystallography structure of CO bound ba3- type cytochrome c oxidase at 2 milliseconds after irradiation by a 532 nm laser
Summary for 8AJZ
| Entry DOI | 10.2210/pdb8ajz/pdb |
| Descriptor | Cytochrome c oxidase subunit 1, Cytochrome c oxidase subunit 2, Cytochrome c oxidase polypeptide IIA, ... (10 entities in total) |
| Functional Keywords | membrane protein, bioenergetics, lipidic cubic phase crystallization, serial femtosecond crystallography, pump- probe method, electron transport |
| Biological source | Thermus thermophilus More |
| Total number of polymer chains | 3 |
| Total formula weight | 92995.23 |
| Authors | Safari, C.,Ghosh, S.,Andersson, R.,Johannesson, J.,Donoso, A.V.,Bath, P.,Bosman, R.,Dahl, P.,Nango, E.,Tanaka, R.,Zoric, D.,Svensson, E.,Nakane, T.,Iwata, S.,Neutze, R.,Branden, G. (deposition date: 2022-07-29, release date: 2023-08-16, Last modification date: 2024-03-20) |
| Primary citation | Safari, C.,Ghosh, S.,Andersson, R.,Johannesson, J.,Bath, P.,Uwangue, O.,Dahl, P.,Zoric, D.,Sandelin, E.,Vallejos, A.,Nango, E.,Tanaka, R.,Bosman, R.,Borjesson, P.,Dunevall, E.,Hammarin, G.,Ortolani, G.,Panman, M.,Tanaka, T.,Yamashita, A.,Arima, T.,Sugahara, M.,Suzuki, M.,Masuda, T.,Takeda, H.,Yamagiwa, R.,Oda, K.,Fukuda, M.,Tosha, T.,Naitow, H.,Owada, S.,Tono, K.,Nureki, O.,Iwata, S.,Neutze, R.,Branden, G. Time-resolved serial crystallography to track the dynamics of carbon monoxide in the active site of cytochrome c oxidase. Sci Adv, 9:eadh4179-eadh4179, 2023 Cited by PubMed Abstract: Cytochrome oxidase (CO) is part of the respiratory chain and contributes to the electrochemical membrane gradient in mitochondria as well as in many bacteria, as it uses the energy released in the reduction of oxygen to pump protons across an energy-transducing biological membrane. Here, we use time-resolved serial femtosecond crystallography to study the structural response of the active site upon flash photolysis of carbon monoxide (CO) from the reduced heme of -type CO. In contrast with the -type enzyme, our data show how CO is stabilized on Cu through interactions with a transiently ordered water molecule. These results offer a structural explanation for the extended lifetime of the Cu-CO complex in -type CO and, by extension, the extremely high oxygen affinity of the enzyme. PubMed: 38064560DOI: 10.1126/sciadv.adh4179 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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