<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Antonyuk SV</submitter><funding>Biotechnology and Biological Sciences Research Council</funding><pagination>15780-5</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC3179090</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>108(38)</volume><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</pubmed_abstract><journal>Proceedings of the National Academy of Sciences of the United States of America</journal><pubmed_title>Carbon monoxide poisoning is prevented by the energy costs of conformational changes in gas-binding haemproteins.</pubmed_title><pmcid>PMC3179090</pmcid><funding_grant_id>B15474</funding_grant_id><funding_grant_id>BB/D01963X/1</funding_grant_id><funding_grant_id>REI20571</funding_grant_id><pubmed_authors>Scrutton NS</pubmed_authors><pubmed_authors>Petersen CA</pubmed_authors><pubmed_authors>Rustage N</pubmed_authors><pubmed_authors>Eady RR</pubmed_authors><pubmed_authors>Antonyuk SV</pubmed_authors><pubmed_authors>Heyes DJ</pubmed_authors><pubmed_authors>Hasnain SS</pubmed_authors><pubmed_authors>Arnst JL</pubmed_authors><pubmed_authors>Sharma R</pubmed_authors><pubmed_authors>Berry NG</pubmed_authors><pubmed_authors>Andrew CR</pubmed_authors></additional><is_claimable>false</is_claimable><name>Carbon monoxide poisoning is prevented by the energy costs of conformational changes in gas-binding haemproteins.</name><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</description><dates><release>2011-01-01T00:00:00Z</release><publication>2011 Sep</publication><modification>2026-04-07T14:13:49.716Z</modification><creation>2019-03-27T00:44:13Z</creation></dates><accession>S-EPMC3179090</accession><cross_references><pubmed>21900609</pubmed><doi>10.1073/pnas.1109051108</doi></cross_references></HashMap>