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“封端”卟啉化合物中的一氧化碳结合动力学

Carbon monoxide binding kinetics in "capped" porphyrin compounds.

作者信息

Rose E J, Venkatasubramanian P N, Swartz J C, Jones R D, Basolo F, Hoffman B M

出版信息

Proc Natl Acad Sci U S A. 1982 Sep;79(18):5742-5. doi: 10.1073/pnas.79.18.5742.

Abstract

The rate constants for CO binding to the five-coordinate ferrous iron complexes of 5,10,15,20-[pyromellitoyl(tetrakis-o-oxyoxyphenyl)]porphyrin and 5,10,15,20-[pyromellitoyl(tetrakis-o-oxypropoxyphenyl)]porphyrin have been measured and compared with the corresponding rate constants for other hemes and hemoproteins. The second-order rate constant is independent of cap size and is comparable to that of high-affinity state hemoglobin (k5 approximately 4 X 10(6) M-1s-1). Therefore, these capped porphyrins provide no steric hindrance to CO binding. In addition, a kinetic scheme involving an unusual seven-coordinate porphyrin species is described.

摘要

已测定了一氧化碳与5,10,15,20-[均苯四甲酰基(四-o-氧代氧基苯基)]卟啉和5,10,15,20-[均苯四甲酰基(四-o-氧代丙氧基苯基)]卟啉的五配位亚铁配合物结合的速率常数,并与其他血红素和血红蛋白的相应速率常数进行了比较。二级速率常数与帽的大小无关,与高亲和力状态血红蛋白的速率常数相当(k5约为4×10⁶ M⁻¹s⁻¹)。因此,这些带帽卟啉对一氧化碳的结合没有空间位阻。此外,还描述了一个涉及不寻常的七配位卟啉物种的动力学方案。

相似文献

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Carbon monoxide binding to iron porphyrins.一氧化碳与铁卟啉的结合。
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Binding of O2 and CO to hemes and hemoproteins.氧气和一氧化碳与血红素及血红蛋白的结合。
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本文引用的文献

4
Carbon monoxide bonding in hemeproteins.
Ann N Y Acad Sci. 1970 Oct 5;174(1):148-53. doi: 10.1111/j.1749-6632.1970.tb49781.x.
7
Conformation and cooperativity in hemoglobin.
Biochemistry. 1975 May 6;14(9):1886-92. doi: 10.1021/bi00680a013.

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