亚硝基苯和苯基异氰化物与螯合的中血红素、血红蛋白及亚铁酞菁的结合。
Bonding of nitrosobenzene and phenyl isocyanide to chelated mesoheme, hemoglobin and ferrous phthalocyanine.
作者信息
Ozaki H, Kinuta M, Matteson J L, Itano H A
机构信息
Department of Pathology, University of California, San Diego, La Jolla 92093.
出版信息
Biochim Biophys Acta. 1988 Jul 20;955(2):220-30. doi: 10.1016/0167-4838(88)90196-3.
Reactions of nitrosobenzene, phenyl isocyanide and their ring-substituted analogues with hemoglobin, ferrous phthalocyanine and a synthetic model compound of hemoglobin were investigated by optical, 1H-NMR and infrared spectroscopy. Complexes of chelated ferromesoheme, the model compound, with 2-methyl-, 2-ethyl, 2-isopropyl- or 2,6-disubstituted nitrosobenzene were less stable than its complex with nitrosobenzene. Formation of a complex of the model compound with 2-tert-butylnitrosobenzene was incomplete. Previous studies showed that 2,6-disubstituted nitrosobenzenes are not ligands of ferrohemoglobin. In the present work 2,6-dimethylphenyl isocyanide was found to be a ligand of ferrohemoglobin. These results are consistent with binding of the nitrogen of the nitroso group of nitrosobenzene and of the carbon of the isocyanide group of phenyl isocyanide to ferroheme. The same bonding modes of these ligands to ferrous phthalocyanine were inferred from ring-current-induced shifts in the 1H-NMR spectra of the respective complexes.
通过光学、1H-NMR和红外光谱研究了亚硝基苯、苯基异氰化物及其环取代类似物与血红蛋白、亚铁酞菁和血红蛋白合成模型化合物的反应。螯合铁卟啉（模型化合物）与2-甲基、2-乙基、2-异丙基或2,6-二取代亚硝基苯形成的配合物比其与亚硝基苯形成的配合物稳定性差。模型化合物与2-叔丁基亚硝基苯形成的配合物不完全。先前的研究表明，2,6-二取代亚硝基苯不是亚铁血红蛋白的配体。在本研究中，发现2,6-二甲基苯基异氰化物是亚铁血红蛋白的配体。这些结果与亚硝基苯亚硝基的氮和苯基异氰化物异氰基的碳与亚铁血红素的结合一致。从各自配合物的1H-NMR光谱中环电流诱导的位移推断出这些配体与亚铁酞菁的相同键合模式。
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