<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Pathak C</submitter><funding>Science and Engineering Research Board</funding><funding>University Grants Commission</funding><funding>Council of Scientific and Industrial Research</funding><pagination>4737-4750</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC6641979</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>2(8)</volume><pubmed_abstract>The active site of the purple acid phosphatase enzyme has been successfully modeled by a series of hetero-dinuclear M(II)-Fe(III) [M = Zn, Ni, Co, and Cu] type complexes of an unsymmetrical [N&lt;sub>6&lt;/sub>O] ligand that contained a bridging phenoxide moiety and one imidazoyl and three pyridyl moieties as the terminal N-binding sites. In particular, the hetero-dinuclear complexes, {L[M&lt;sup>II&lt;/sup>(μ-OAc)&lt;sub>2&lt;/sub>Fe&lt;sup>III&lt;/sup>]}(ClO&lt;sub>4&lt;/sub>)&lt;sub>2&lt;/sub> [M = Zn (&lt;b>3a&lt;/b>), Ni (&lt;b>3b&lt;/b>), Co (&lt;b>4a&lt;/b>), and Cu (&lt;b>4b&lt;/b>)], were obtained directly from the phenoxy-bridged ligand (HL), namely 2-{[bis(2-methylpyridyl)amino]methyl}-6-{[((1-methylimidazol-2-yl)methyl)(2-pyridylmethyl)amino]methyl}-4-&lt;i>t&lt;/i>-butylphenol (&lt;b>2&lt;/b>), upon sequential addition of Fe(ClO&lt;sub>4&lt;/sub>)&lt;sub>3</pubmed_abstract><journal>ACS omega</journal><pubmed_title>Modeling the Active Site of the Purple Acid Phosphatase Enzyme with Hetero-Dinuclear Mixed Valence M(II)-Fe(III) [M = Zn, Ni, Co, and Cu] Complexes Supported over a [N&lt;sub>6&lt;/sub>O] Unsymmetrical Ligand.</pubmed_title><pmcid>PMC6641979</pmcid><funding_grant_id>EMR/2014/000254</funding_grant_id><pubmed_authors>Prakasham AP</pubmed_authors><pubmed_authors>Pathak C</pubmed_authors><pubmed_authors>Gangwar MK</pubmed_authors><pubmed_authors>Gupta SK</pubmed_authors><pubmed_authors>Ghosh P</pubmed_authors></additional><is_claimable>false</is_claimable><name>Modeling the Active Site of the Purple Acid Phosphatase Enzyme with Hetero-Dinuclear Mixed Valence M(II)-Fe(III) [M = Zn, Ni, Co, and Cu] Complexes Supported over a [N&lt;sub>6&lt;/sub>O] Unsymmetrical Ligand.</name><description>The active site of the purple acid phosphatase enzyme has been successfully modeled by a series of hetero-dinuclear M(II)-Fe(III) [M = Zn, Ni, Co, and Cu] type complexes of an unsymmetrical [N&lt;sub>6&lt;/sub>O] ligand that contained a bridging phenoxide moiety and one imidazoyl and three pyridyl moieties as the terminal N-binding sites. In particular, the hetero-dinuclear complexes, {L[M&lt;sup>II&lt;/sup>(μ-OAc)&lt;sub>2&lt;/sub>Fe&lt;sup>III&lt;/sup>]}(ClO&lt;sub>4&lt;/sub>)&lt;sub>2&lt;/sub> [M = Zn (&lt;b>3a&lt;/b>), Ni (&lt;b>3b&lt;/b>), Co (&lt;b>4a&lt;/b>), and Cu (&lt;b>4b&lt;/b>)], were obtained directly from the phenoxy-bridged ligand (HL), namely 2-{[bis(2-methylpyridyl)amino]methyl}-6-{[((1-methylimidazol-2-yl)methyl)(2-pyridylmethyl)amino]methyl}-4-&lt;i>t&lt;/i>-butylphenol (&lt;b>2&lt;/b>), upon sequential addition of Fe(ClO&lt;sub>4&lt;/sub>)&lt;sub>3</description><dates><release>2017-01-01T00:00:00Z</release><publication>2017 Aug</publication><modification>2025-05-18T13:15:40.564Z</modification><creation>2025-05-18T13:15:40.564Z</creation></dates><accession>S-EPMC6641979</accession><cross_references><pubmed>31457757</pubmed><doi>10.1021/acsomega.7b00671</doi></cross_references></HashMap>