Ligand discrimination of myoglobin in solution: an iron L-edge X-ray absorption study of the active centre-Reference-Cited by-同舟云学术

Ligand discrimination of myoglobin in solution: an iron L-edge X-ray absorption study of the active centre

Published:2013 Issue:39 Volume:49 Page:4163-4165
ISSN:1359-7345
Container-title:Chemical Communications
language:en
Short-container-title:Chem. Commun.

Author:

Lange Kathrin M.¹²³,Golnak Ronny⁴⁵²³,Bonhommeau Sébastien⁶⁷⁸,Aziz Emad F.⁴⁵²³⁹

Affiliation:

1. Max-Born-Institut

2. 12489 Berlin

3. Germany

4. Joint Ultrafast Dynamics Lab in Solutions and at Interfaces (JULiq)

5. Helmholtz-Zentrum Berlin für Materialien und Energie

6. Université de Bordeaux

7. Institut des Sciences Moléculaires

8. France

9. Freie Universität Berlin

Abstract

Iron L-edge X-ray absorption spectra of the active centre of myoglobin in the met-form, in the reduced form and upon ligation to O₂, CO, NO and CN are presented.

Publisher

Royal Society of Chemistry (RSC)

Subject

Materials Chemistry,Metals and Alloys,Surfaces, Coatings and Films,General Chemistry,Ceramics and Composites,Electronic, Optical and Magnetic Materials,Catalysis

Link

http://pubs.rsc.org/en/content/articlepdf/2013/CC/C3CC37973F

Reference31 articles.

1. Discovery of new ligand binding pathways in myoglobin by random mutagenesis

2. Atomic level computational identification of ligand migration pathways between solvent and binding site in myoglobin

3. Synthetic Models for Hemoglobin and Myoglobin

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