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- W2084133020 abstract "The geometric and electronic structure of NO bound to reduced protocatechuate 3,4-dioxygenase and its substrate (3,4-dihydroxybenzoate, PCA) complex have been examined by X-ray absorption (XAS), UV−vis absorption (Abs), magnetic circular dichroism (MCD), and variable temperature variable field (VTVH) MCD spectroscopies. The results are compared to those previously published on model complexes described as {FeNO}7 systems in which an S = 5/2 ferric center is antiferromagnetically coupled to an S = 1 NO-. XAS pre-edge analysis indicates that the Fe−NO units in FeIIIPCD{NO-} and FeIIIPCD{PCA,NO-} lack the greatly increased pre-edge intensity representative of most {FeNO}7 model sites. Furthermore, from extended X-ray absorption fine structure (EXAFS) analysis, the FeIIIPCD{NO-} and FeIIIPCD{PCA,NO-} active sites are shown to have an Fe−NO distance of at least 1.91 Å, ≈0.2 Å greater than those found in the model complexes. The weakened Fe−NO bond is consistent with the overall lengthening of the bond lengths and the fact that VTVH MCD data show that NO- → FeIII CT transitions are no longer polarized along the z-axis of the zero-field splitting tensor. The weaker Fe−NO bond derives from the strong donor interaction of the endogenous phenolate and substrate catecholate ligands, which is observed from the increased intensity in the CT region relative to that of {FeNO}7 model complexes, and from the shift in XAS edge position to lower energy. As NO is an analogue of O2, the effect of endogenous ligand donor strength on the Fe−NO bond has important implications with respect to O2 activation by non-heme iron enzymes." @default.
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- W2084133020 date "2002-12-17" @default.
- W2084133020 modified "2023-10-16" @default.
- W2084133020 title "Spectroscopic Studies of the Effect of Ligand Donor Strength on the Fe−NO Bond in Intradiol Dioxygenases" @default.
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- W2084133020 doi "https://doi.org/10.1021/ic025906f" @default.
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