<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>2(12)</volume><submitter>Watanabe K</submitter><pubmed_abstract>All fundamental data about binding of the cyanide to a supramolecular complex composed of a per-O-methylated β-cyclodextrin dimer having an imidazole linker (Im3CD) and an anionic ferric porphyrin (Fe((III))TPPS) indicate that the Fe((III))TPPS/Im3CD complex is much better as an cyanide receptor in vivo than hydroxocobalamin, whose cyanide binding ability is lowered by its strong binding to serum proteins in the blood.</pubmed_abstract><journal>ACS medicinal chemistry letters</journal><pagination>943-7</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC4018087</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Supramolecular ferric porphyrins as cyanide receptors in aqueous solution.</pubmed_title><pmcid>PMC4018087</pmcid><pubmed_authors>Kano K</pubmed_authors><pubmed_authors>Kitagishi H</pubmed_authors><pubmed_authors>Watanabe K</pubmed_authors></additional><is_claimable>false</is_claimable><name>Supramolecular ferric porphyrins as cyanide receptors in aqueous solution.</name><description>All fundamental data about binding of the cyanide to a supramolecular complex composed of a per-O-methylated β-cyclodextrin dimer having an imidazole linker (Im3CD) and an anionic ferric porphyrin (Fe((III))TPPS) indicate that the Fe((III))TPPS/Im3CD complex is much better as an cyanide receptor in vivo than hydroxocobalamin, whose cyanide binding ability is lowered by its strong binding to serum proteins in the blood.</description><dates><release>2011-01-01T00:00:00Z</release><publication>2011 Dec</publication><modification>2025-04-05T10:20:32.853Z</modification><creation>2019-03-27T01:28:02Z</creation></dates><accession>S-EPMC4018087</accession><cross_references><pubmed>24900285</pubmed><doi>10.1021/ml200231x</doi></cross_references></HashMap>