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- W2140163721 abstract "Abstract Catecholate‐Fe(III) (high‐spin) bonds are important in many areas of bioinorganic chemistry. These exhibit low‐energy, intense ligand‐to‐metal charge transfer (LMCT) transitions reflecting highly covalent bonds. This high covalency can make a major contribution to function. In this review, we develop the method of metal L‐edge X‐ray absorption spectroscopy (XAS) as a probe of differential orbital covalency (DOC), the amount of ligand character in the different d orbitals of a metal site in a highly covalent environment. We then apply this method to experimentally determine the covalency of the ligand‐metal bonds related to the siderophores and computationally evaluate this contribution to their high stability constants. We then use variable‐temperature, variable‐field, magnetic circular dichroism (VTVH MCD) spectroscopy to assign the LMCT transitions of the catecholate‐, substrate‐bound Fe III site of the intradiol dioxygenases. A reaction coordinate is presented where this charge transfer can overcome the spin‐forbidden nature of the reaction of the bound catecholate (singlet) with dioxygen (triplet)." @default.
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- W2140163721 date "2011-12-15" @default.
- W2140163721 modified "2023-10-03" @default.
- W2140163721 title "Nature of the Catecholate-Fe(III) Bond: High Affinity Binding and Substrate Activation in Bioinorganic Chemistry" @default.
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- W2140163721 doi "https://doi.org/10.1002/9781119951438.eibc0404" @default.
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