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- W127968479 abstract "1H nuclear magnetic resonance longitudinal relaxation time (T1) measurements were used to study the interaction of xylidine with solubilized rat liver microsomal cytochrome P450, myoglobin and hemoglobin, and to study the binding of aniline and imidazole to human hemoglobin. Since the carboxyferrous derivatives of all three hemoproteins are diamagnetic, they were used in all cases to give control values (1/T10) which allowed calculation of the paramagnetic relaxation rate values (1/T1p) where 1/T1p represents the specific paramagnetic effect of Fe3+ upon the relaxation rate of the substrate. Upon addition of ferricytochrome P450, ferrimyoglobin, or ferrihemoglobin to solutions of xylidine, the T1 values for the methyl and phenyl moieties of the xylidine molecule decreased markedly relative to the control conditions. The observed changes showed that xylidine was much more sensitive to cytochrome P450 than to myoglobin or hemoglobin; and whereas myoglobin produced essentially the same effect upon the relaxation rates of the phenyl and methyl protons, hemoglobin and cytochrome P450 produced differential changes, phenyl > methyl. Such T1 data in conjunction with values (obtained separately) of the dissociation constants (KS) and estimates of the correlation times (τC) for the various complexes allowed calculations of distances between the heme iron atoms and specific portions of the complexed substrate molecules. These estimates suggested that xylidine may not be an inner sphere ligand of solubilized P450. Similar results obtained for aniline and imidazole with hemoglobin would suggest that these substrates are directly coordinated. Further distinctions among the complexes were obtained when CN− or F− were added along with the substrates and ferrihemoproteins; these ligands apparently displaced imidazole from hemoglobin, but they did not abolish the interaction of xylidine or of aniline with hemoglobin." @default.
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- W127968479 date "1977-01-01" @default.
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- W127968479 title "NMR RELAXATION TIME STUDIES OF SUBSTRATE INTERACTIONS WITH P450 AND OTHER HEMOPROTEINS" @default.
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- W127968479 doi "https://doi.org/10.1016/b978-0-08-021523-5.50036-5" @default.
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