Assignment of the axial ligands of the haem in milk lactoperoxidase using magnetic circular dichroism spectroscopy
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics,Structural Biology
Reference39 articles.
1. Bovine Lactoperoxidase. Partial Characterization of the Further Purified Protein*
2. Physical and Compositional Investigations of the Subfractions of Lactoperoxidase.
3. The prosthetic group of milk lactoperoxidase is protoheme IX
4. Structure of milk lactoperoxidase
5. Biology of the Mouth;Morrison,1968
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1. Spectroscopic Evidence of the Role of an Axial Ligand Histidinate in the Mechanism of Adrenal Cytochrome b561;Biochemistry;2012-10-29
2. The Met243 sulfonium ion linkage is responsible for the anomalous magnetic circular dichroism and optical spectral properties of myeloperoxidase;JBIC Journal of Biological Inorganic Chemistry;1999-12
3. The Active Form of the Ferric Heme in Neutrophil Cytochrome b558 Is Low-Spin in the Reconstituted Cell-Free System in the Presence of Amphophil;Journal of Biochemistry;1999-10-01
4. Spectral Analysis of Lactoperoxidase;Journal of Biological Chemistry;1996-02
5. Evidence for the high-spin heme iron in both stable and unstable reduced forms of lactoperoxidase: low-temperature magnetic circular dichroism data;FEBS Letters;1995-12-27
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