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Updated: Oct 4, 2026

Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092
Published on: October 2, 2017
Quantitative analysis of x-ray absorption near edge structure data by a full multiple scattering procedure: the Fe-CO
S Della Longa1, A Arcovito, M Girasole
1Dipartimento Medicina Sperimentale, Università L'Aquila, 67100 L'Aquila, Italy.
Abstract:
We report the first quantitative analysis of the Fe K-edge polarized x-ray absorption near edge structure of the iron protein carbonmonoxy-myoglobin (MbCO) single crystal and of its cryogenic photoproduct Mb(*)CO. The CO-Fe-heme local structure has been determined using a novel fitting procedure based on the full multiple scattering approach. The extracted local structure of Mb(*)CO includes a Fe-CO distance of (3.08+/-0.07) A, with a tilting angle between the heme normal and the Fe-C vector of (37+/-7) degrees, and a bending angle between the Fe-C vector and the C-O bond of (31+/-5) degrees.
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