| Literature DB >> 11580707 |
S Della Longa1, A Arcovito, M Girasole, J L Hazemann, M Benfatto.
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.Entities:
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Year: 2001 PMID: 11580707 DOI: 10.1103/PhysRevLett.87.155501
Source DB: PubMed Journal: Phys Rev Lett ISSN: 0031-9007 Impact factor: 9.161