Preparation and Initial Characterization of the Compound I, II, and III States of Iron Methylchlorin-Reconstituted Horseradish Peroxidase and Myoglobin: Models for Key Intermediates in Iron Chlorin Enzymes
- 29 December 2000
- journal article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 279 (3) , 1011-1015
- https://doi.org/10.1006/bbrc.2000.4077
Abstract
No abstract availableKeywords
This publication has 38 references indexed in Scilit:
- Structures of the Siroheme- and Fe4S4-Containing Active Center of Sulfite Reductase in Different States of Oxidation: Heme Activation via Reduction-Gated Exogenous Ligand Exchange,Biochemistry, 1997
- Heme-Containing OxygenasesChemical Reviews, 1996
- Crystal structure of catalase HPII from Escherichia coliStructure, 1995
- The oxygenated complex of cytochrome d terminal oxidase: direct evidence for iron-oxygen coordination in a chlorin-containing enzyme by resonance Raman spectroscopyJournal of the American Chemical Society, 1993
- The active site structure ofE. coliHPII catalaseFEBS Letters, 1991
- The cytochromes of anaerobically grown Escherichia coli. An electron-paramagnetic-resonance study of the cytochrome bd complex in situBiochemical Journal, 1989
- Proton NMR characterization of isomeric sulfmyoglobins: preparation, interconversion, reactivity patterns, and structural featuresBiochemistry, 1987
- The cytochromes ofEscherichia coliFEMS Microbiology Letters, 1987
- Electron flow and heme-heme interaction between cytochromes b-558, b-595 and d in a terminal oxidase of Escherichia coliBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1987
- Catalase of Neurospora crassa. 1. Induction, purification, and physical propertiesBiochemistry, 1979