乙酰糖基金属卟啉的合成及其对烷烃温和氧化的选择性催化作用

Synthesis of Glycoconjugated Metalloporphyrins and Their Selective Catalysis for Alkane Oxidation Under Mild Conditions

由吡咯和葡萄糖取代苯甲醛直接缩合制备了两种葡萄糖取代卟吩,四(邻位乙酸葡萄糖氧代苯基)卟吩和四(间位乙酰葡萄糖氧代苯基)卟吩,它们进一步金属化合成了四种葡萄糖金属卟啉,氯化四(邻位乙酰葡萄糖氧代苯基)卟吩合铁、氯化四(间位乙酰葡萄糖氧代苯基)卟吩合铁、氯化四(邻位四乙酰葡萄糖氧代苯基)卟吩合锰和氯化四(间位乙酰葡萄糖氧代苯基)卟吩合锰.它们的结构由紫外-可见光谱、元素分析和核磁共振证实.研究了这些葡萄糖取代金属卟啉对亚碘酰苯常温常压下氧化异戊烷反应的选择性催化作用.研究表明,糖基金属卟啉催化异戊烷端基碳氢键的氧化,对一级碳氢键表现出专一性催化作用.非糖基金属卟啉催化异戊烷二级和三级碳氢键的氧化.与非糖基金属卟啉比较,糖基金属卟啉对烷烃羟基化反应的催化行为更接近细胞色素P-450单充氧酶.

Two glycoconjugated porphines, tetra[2-acetylglucosyl-oxo-phenyl]porphine [T( o-glu)PPH2] and tetra[3-acerylglycosy-oxo-phenyl]porphine[T(m-glu)PPH2] ,were synthesized from the reaction of pyrrole with ortho-acetylglycosylate benzaldehyde and meta - acetylglycosylate benzaldehyde, respectively, by using Lindsey' s method. Four glycoconjugated metalloporphyrins, chloro [ tetra ( o-2, 3, 4, 6-O-acetylglucose-1-O-phenyl) porphinato ] iron [ T ( o-glu) PPFeCl ], chloro [ tetra ( o-2, 3, 4, 6-O-acetylglucose-l-O-phenyl) porphinato] manganese, [ T ( o-glu ) PPMnCl ], chloro [ tetra ( m-2, 3,4, 6-O-acetylglucose-l-O-phenyl) porphinato]iron [T( m-glu)PPFeCl] and chloro[ tetra( m-2, 3,4,6-O-acetylglucose-l-O-phenyl) porphinato] manganese [T(m-glu)PPMnCl] were prepared from these glycoconjugated porphines. The newly synthesized compounds were characterized by UV-vis spectroscopy, elemental analysis and 1H NMR.The catalytic oxidation of 2-methylbutane with PhIO as an oxidant at room temperature and under atmospheric pressure by four glycoconjugated metalloporphyrins was studied. The research showed that glycoconjugated metalloporphyrins catalyzed regiospecifically the hydroxylation of the primary carbon-hydrogen bonds of 2-methylbutane, and that non-glycoconjugated metalloporphyrins catalyzed selectively the oxidation of secondary and tertiary carbon-hydrogen bonds of 2-methylbutane. hi contrast with metalloporphyrins without sugar groups, the selective catalysis of these glycoconjugated metalloporphyrins for hydrocarbon oxidation was closer to cytochrome P - 450monooxygenase.