The effect of structural disorder on the X-ray absorption near-edge structure (XANES) spectrum of a heme protein has been investigated using the dynamical description of the system derived from molecular dynamics (MD) simulations. The XANES spectra of neuroglobin (Ngb) and carbonmonoxy-neuroglobin (NgbCO) have been quantitatively reproduced, starting from the MD geometrical configurations, without carrying out any optimization in the structural parameter space. These results provide an important experimental validation of the reliability of the potentials used in the MD simulations and accordingly corroborate the consistency of the structural dynamic information on the metal center, related to its biological function. This analysis allowed us to demonstrate that the configurational disorder associated with the distortion of the heme plane and with the different orientations of the axial ligands can affect the XANES features at very low energy. Neglecting configurational disorder in the XANES quantitative analysis of heme proteins is a source of systematic errors in the determination of Fe coordination geometry. The combined use of XANES and MD is a novel strategy to enhance the resolution and reliability of the structural information obtained on metalloproteins, making the combination of these techniques powerful for metalloprotein investigations.

Dynamic Investigation of Protein Metal Active Sites: Interplay of XANES and Molecular Dynamics Simulations / D'Angelo, Paola; Stefano Della, Longa; Alessandro, Arcovito; Anselmi, Massimiliano; DI NOLA, Alfredo; Giovanni, Chillemi. - In: JOURNAL OF THE AMERICAN CHEMICAL SOCIETY. - ISSN 0002-7863. - STAMPA. - 132:42(2010), pp. 14901-14909. [10.1021/ja1056533]

Dynamic Investigation of Protein Metal Active Sites: Interplay of XANES and Molecular Dynamics Simulations

D'ANGELO, Paola;ANSELMI, MASSIMILIANO;DI NOLA, Alfredo;
2010

Abstract

The effect of structural disorder on the X-ray absorption near-edge structure (XANES) spectrum of a heme protein has been investigated using the dynamical description of the system derived from molecular dynamics (MD) simulations. The XANES spectra of neuroglobin (Ngb) and carbonmonoxy-neuroglobin (NgbCO) have been quantitatively reproduced, starting from the MD geometrical configurations, without carrying out any optimization in the structural parameter space. These results provide an important experimental validation of the reliability of the potentials used in the MD simulations and accordingly corroborate the consistency of the structural dynamic information on the metal center, related to its biological function. This analysis allowed us to demonstrate that the configurational disorder associated with the distortion of the heme plane and with the different orientations of the axial ligands can affect the XANES features at very low energy. Neglecting configurational disorder in the XANES quantitative analysis of heme proteins is a source of systematic errors in the determination of Fe coordination geometry. The combined use of XANES and MD is a novel strategy to enhance the resolution and reliability of the structural information obtained on metalloproteins, making the combination of these techniques powerful for metalloprotein investigations.
2010
01 Pubblicazione su rivista::01a Articolo in rivista
Dynamic Investigation of Protein Metal Active Sites: Interplay of XANES and Molecular Dynamics Simulations / D'Angelo, Paola; Stefano Della, Longa; Alessandro, Arcovito; Anselmi, Massimiliano; DI NOLA, Alfredo; Giovanni, Chillemi. - In: JOURNAL OF THE AMERICAN CHEMICAL SOCIETY. - ISSN 0002-7863. - STAMPA. - 132:42(2010), pp. 14901-14909. [10.1021/ja1056533]
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11573/44676
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