Cation Binding by the Phenolate Group in Small Molecules and Proteins

Autor:	Pinak Chakrabarti, Barbara T. Hsu
Rok vydání:	1994
Předmět:	Cation binding Stereochemistry Chemistry Hydrogen bond Metal ions in aqueous solution Small molecule Inorganic Chemistry Metal visual_art visual_art.visual_art_medium Side chain Physical and Theoretical Chemistry Tyrosine Lone pair
Zdroj:	Inorganic Chemistry. 33:1165-1170
ISSN:	1520-510X 0020-1669
DOI:	10.1021/ic00084a032
Popis:	The geometry of interactions of metal ions with the phenolate group in proteins and small molecules has been examined using coordinates listed in structural databases. Cations are found to avoid the sp^2 lone pair directions of the ligand oxygen; in small-molecule structures most of the cations are clustered close to the aromatic plane in the region between the sp^2 and the C-O vectors, whereas in proteins the ions move out of the plane. Such a spatial distribution is different from that observed for hydrogen-bonded neighbors interacting with a neutral tyrosine residue. The environment of a tyrosinate anion is such that it has a cation on one side of its plane and a hydrogen-bond donor on the other. Metal binding can disturb the normal conformation of the tyrosine side chain.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::179766ff637c64a9b446918132580766 https://doi.org/10.1021/ic00084a032 Zobrazit plný text záznamu