{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Antonyuk SV"],"funding":["Biotechnology and Biological Sciences Research Council"],"pagination":["15780-5"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3179090"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["108(38)"],"pubmed_abstract":["Carbon monoxide (CO) is a product of haem metabolism and organisms must evolve strategies to prevent endogenous CO poisoning of haemoproteins. We show that energy costs associated with conformational changes play a key role in preventing irreversible CO binding. AxCYTcp is a member of a family of haem proteins that form stable 5c-NO and 6c-CO complexes but do not form O(2) complexes. Structure of the AxCYTcp-CO complex at 1.25 Å resolution shows that CO binds in two conformations moderated by the extent of displacement of the distal residue Leu16 toward the haem 7-propionate. The presence of two CO conformations is confirmed by cryogenic resonance Raman data. The preferred linear Fe-C-O arrangement (170 ± 8°) is accompanied by a flip of the propionate from the distal to proximal face of th"],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pubmed_title":["Carbon monoxide poisoning is prevented by the energy costs of conformational changes in gas-binding haemproteins."],"pmcid":["PMC3179090"],"funding_grant_id":["B15474","BB/D01963X/1","REI20571"],"pubmed_authors":["Scrutton NS","Petersen CA","Rustage N","Eady RR","Antonyuk SV","Heyes DJ","Hasnain SS","Arnst JL","Sharma R","Berry NG","Andrew CR"],"additional_accession":[]},"is_claimable":false,"name":"Carbon monoxide poisoning is prevented by the energy costs of conformational changes in gas-binding haemproteins.","description":"Carbon monoxide (CO) is a product of haem metabolism and organisms must evolve strategies to prevent endogenous CO poisoning of haemoproteins. We show that energy costs associated with conformational changes play a key role in preventing irreversible CO binding. AxCYTcp is a member of a family of haem proteins that form stable 5c-NO and 6c-CO complexes but do not form O(2) complexes. Structure of the AxCYTcp-CO complex at 1.25 Å resolution shows that CO binds in two conformations moderated by the extent of displacement of the distal residue Leu16 toward the haem 7-propionate. The presence of two CO conformations is confirmed by cryogenic resonance Raman data. The preferred linear Fe-C-O arrangement (170 ± 8°) is accompanied by a flip of the propionate from the distal to proximal face of th","dates":{"release":"2011-01-01T00:00:00Z","publication":"2011 Sep","modification":"2026-04-07T14:13:49.716Z","creation":"2019-03-27T00:44:13Z"},"accession":"S-EPMC3179090","cross_references":{"pubmed":["21900609"],"doi":["10.1073/pnas.1109051108"]}}