A Schiff-base porphyrin complex with double intramolecular hydrogen bonds

被引：10

作者：

Huang, Wei ^{[1
]}

Jiang, Jiaxun ^{[1
]}

Feng, Zhiqiang ^{[1
]}

Kai, Xiaoxu ^{[1
]}

Hu, Chuanjiang ^{[1
,2
,3
]}

Yu, Hong ^{[1
]}

Yang, Wen ^{[1
]}

机构：

[1] Soochow Univ, Coll Chem Chem Engn & Mat Sci, Key Lab Organ Synth Jiangsu Prov, Suzhou 215123, Peoples R China

[2] Nanjing Univ, State Key Lab, Nanjing 210093, Peoples R China

[3] Nanjing Univ, Inst Coordinat Chem, Nanjing 210093, Peoples R China

来源：

JOURNAL OF COORDINATION CHEMISTRY | 2011年 / 64卷 / 12期

关键词：

Porphyrin; Intramolecular hydrogen bond; Schiff base; Salicylideneaminophenyl; Binding constant; PROTON-TRANSFER; HORSERADISH-PEROXIDASE; CRYSTAL-STRUCTURE; PROXIMAL LIGAND; MODELS; SUBSTITUTION; FLUORESCENCE; MECHANISMS; MYOGLOBIN; PROTEINS;

D O I：

10.1080/00958972.2011.589002

中图分类号：

O61 [无机化学];

学科分类号：

070301 ; 081704 ;

摘要：

We have designed a porphyrin with a Schiff-base substituent as a model to study intramolecular hydrogen-bonding. The corresponding complex [Zn(SATPP)(CH3OH)] has been synthesized and characterized by X-ray crystallography, H-1 NMR, and UV-Vis spectroscopy. The structure shows that there are three phenyl groups and one salicylideneaminophenyl group at the meso positions of the porphyrin, and the phenol oxygen is involved in double hydrogen bonds, one within the salicylideneaminophenyl and the other between coordinated methanol and phenol oxygen. H-1 NMR spectra suggest that the binding of methanol to zinc is an equilibrium process in solution and the equilibrium constant has been determined by UV-Vis measurements. The intramolecular hydrogen bond stabilizes the structure, and the binding affinity increases 10 times over the corresponding TPP (TPP, dianion of meso-5,10,15,20-tetraphenylporphyrin).

引用

页码：2101 / 2109

页数：9

共 34 条

[1] ROLES OF PROXIMAL LIGAND IN HEME-PROTEINS - REPLACEMENT OF PROXIMAL HISTIDINE OF HUMAN MYOGLOBIN WITH CYSTEINE AND TYROSINE BY SITE-DIRECTED MUTAGENESIS AS MODELS FOR P-450, CHLOROPEROXIDASE, AND CATALASE [J].