Quantitative analysis of x-ray absorption near edge structure data by a full multiple scattering procedure: the Fe-CO geometry in photolyzed carbonmonoxy-myoglobin single crystal

Alessandro Arcovito, S Della Longa, M Girasole, Jl Hazemann, M. Benfatto

Risultato della ricerca: Contributo in rivistaArticolo in rivistapeer review

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.
Lingua originaleEnglish
pagine (da-a)155501-155501
Numero di pagine1
RivistaPhysical Review Letters
Volume87
Stato di pubblicazionePubblicato - 2001

Keywords

  • Animals
  • Binding Sites
  • Carbon Monoxide
  • Crystallography, X-Ray
  • Heme
  • Iron
  • Myoglobin
  • Photolysis
  • Protein Conformation
  • Scattering, Radiation
  • Spectrometry, X-Ray Emission
  • Whales

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