Abstract
The active site geometry of Fe(II)-bleomycin, peplomycin and its derivatives have been studied on the basis of theoretical multiple scattering simulations of the Fe K-edge x-ray absorption near edge structure. Comparisons of the experimental and theoretical spectra calculated for the different models of Fe(II)-bleomycin reveal serious distortions of the ligands nearest to Fe. This includes the presence of one ligand with a very short bond length as well as angular distortions. Reconstruction of the nearest environment of the Fe during perturbation of axial ligand was investigated for peplomycin. It was found that replacement of carbamoyl group of the mannose with solvent molecule led to a small increase of average radius (0.03 Å) of the first atomic shell around Fe ion and elongation of the shortest bond length (0.10 Å).
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