期刊
INORGANIC CHEMISTRY
卷 60, 期 5, 页码 3207-3217出版社
AMER CHEMICAL SOC
DOI: 10.1021/acs.inorgchem.0c03548
关键词
-
资金
- JSPS [17H03032, 19H04581]
- CREST
- Grants-in-Aid for Scientific Research [19H04581, 17H03032] Funding Source: KAKEN
The study compared the reactivity of meso-tetramesitylporphyrin and 2,7,12,17-tetramethyl-3,8,13,18-tetramesitylporphyrin for different reactions, revealing that the former is more reactive under non-sterically bulky substrate conditions, but the reactivity becomes similar when the substrate becomes sterically hindered. Density functional theory calculations showed differences in the orbital energies of the Fe=O moiety between the two porphyrins.
There have been two known categories of porphyrins: a meso-substituted porphyrin like meso-tetramesitylporphyrin (TMP) and a pyrrole-beta-substituted porphyrin like native porphyrins and 2,7,12,17-tetramethyl-3,8,13,18-tetramesitylporphyrin (TMTMP). To reveal the chemical and biological function of native hemes, we compare the reactivity of the oxoiron(IV) porphyrin pi-cation radical complex (Compound I) of TMP (TMP-1) with that of TMTMP (TMTMP-I) for epoxidation, hydrogen abstraction, hydroxylation, sulfoxidation, and demethylation reactions. Kinetic analysis of these reactions indicated that TMP-I is much more reactive than TMTMP-I when the substrate is not sterically bulky. However, as the substrate is sterically bulkier, the difference of the reactivity between TMP-I and TMTMP-I becomes smaller, and the reactivity of TMP-I is comparable to that of TMTMP-I for a sterically hindered substrate. Since the redox potential of TMP-I is almost the same as that of TMTMP-I, we conclude that TMP-I is intrinsically more reactive than TMTMP-I for these atom transfer reactions, but the steric effect of TMP-I is stronger than that of TMTMP-I. This is contrary to the previous result for the single electron transfer reaction: TMTMP-I is faster than TMP-I. DFT calculations indicate that the orbital energies of the Fe=O moiety for TMTMP-I are higher than those for TMP-I. The difference in steric effect between TMP-I and TMTMP-I is explained by the distance from the mesityl group to the oxo ligand of Compound I. Significance of the pyrrole-beta-substituted structure of the hemes in native enzymes is also discussed on the basis of this study.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据