High-Energy-Resolution Fluorescence-Detected X-ray Absorption of the Q Intermediate of Soluble Methane Monooxygenase.

ABSTRACT: Kα high-energy-resolution fluorescence detected X-ray absorption spectroscopy (HERFD XAS) provides a powerful tool for overcoming the limitations of conventional XAS to identify the electronic structure and coordination environment of metalloprotein active sites. Herein, Fe Kα HERFD XAS is applied to the diiron active site of soluble methane monooxygenase (sMMO) and to a series of high-valent diiron model complexes, including diamond-core [Fe^IV₂(μ-O)₂(L)₂](ClO₄)₄] (3) and open-core [(O═Fe^IV-O-Fe^IV(OH)(L)₂](ClO₄)₃ (4) models (where, L = tris(3,5-dimethyl-4-methoxypyridyl-2-methyl)amine) (TPA*)). Pronounced differences in the HERFD XAS pre-edge energies and intensities are

SUBMITTER: Castillo RG 

PROVIDER: S-EPMC5729100 | biostudies-literature | 2017 Dec

REPOSITORIES: biostudies-literature