Iron Oxidation State Modulates Active Site Structure in a Heme Peroxidase,-Reference-Cited by-同舟云学术

Iron Oxidation State Modulates Active Site Structure in a Heme Peroxidase,

Published:2008-03-20 Issue:15 Volume:47 Page:4403-4409
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Badyal Sandip K.¹,Metcalfe Clive L.¹,Basran Jaswir¹,Efimov Igor¹,Moody Peter C. E.¹,Raven Emma Lloyd¹

Affiliation:

1. Department of Chemistry, Henry Wellcome Building, University of Leicester, University Road, Leicester LE1 7RH, England, U.K., and Department of Biochemistry and Henry Wellcome Laboratories for Structural Biology, Henry Wellcome Building, University of Leicester, Lancaster Road, Leicester LE1 9HN, England, U.K.

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi702337n

Reference30 articles.

1. Proton-Linked Protein Conformational Switching: Definition of the Alkaline Conformational Transition of Yeast Iso-1-ferricytochrome c

2. Identification of the Ligands to the Ferric Heme of Chlamydomonas Chloroplast Hemoglobin: Evidence for Ligation of Tyrosine-63 (B10) to the Heme

3. Haem-ligand switching during catalysis in crystals of a nitrogen-cycle enzyme

4. Structural Basis for the Mechanism of Ca2+ Activation of the Di-Heme Cytochrome c Peroxidase from Pseudomonas nautica 617

5. The Interaction of Covalently Bound Heme with the Cytochrome c Maturation Protein CcmE

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