Ferric α-Hydroxyheme Bound to Heme Oxygenase Can Be Converted to Verdoheme by Dioxygen in the Absence of Added Reducing Equivalents
Open Access
- 1 June 1999
- journal article
- Published by Elsevier
- Vol. 274 (26), 18196-18200
- https://doi.org/10.1074/jbc.274.26.18196
Abstract
No abstract availableKeywords
This publication has 19 references indexed in Scilit:
- Solution1H NMR Investigation of the Molecular and Electronic Structure of the Active Site of Substrate-Bound Human Heme Oxygenase: the Nature of the Distal Hydrogen Bond Donor to Bound LigandsJournal of the American Chemical Society, 1998
- Cobalt Porphyrin Heme Oxygenase Complex. EPR Evidences for the Distal Heme Pocket Hydrogen BondingJournal of the American Chemical Society, 1998
- Heme Oxygenase-1, Intermediates in Verdoheme Formation and the Requirement for Reduction EquivalentsJournal of Biological Chemistry, 1997
- Resonance Raman Spectroscopic Characterization of α-Hydroxyheme and Verdoheme Complexes of Heme OxygenaseBiochemistry, 1997
- Studies on the Iron(II) meso-Oxyporphyrin .pi.-Neutral Radical as a Reaction Intermediate in Heme CatabolismInorganic Chemistry, 1995
- Identification of Histidine 25 as the Heme Ligand in Human Liver Heme OxygenaseBiochemistry, 1994
- NMR studies of metalloporphyrin radicals. Iron(II) oxophlorin radical formed from iron(III) meso-hydroxyoctaethylporphyrinJournal of the American Chemical Society, 1986
- The EPR of low spin heme complexes Relation of the τ2g hole model to the directional properties of the g tensor, and a new method for calculating the ligand field parametersBiochimica et Biophysica Acta (BBA) - Protein Structure, 1977
- Reactions of oxophlorines and their .pi. radicalsJournal of the American Chemical Society, 1975
- Low—Spin Compounds of Heme ProteinsPublished by American Chemical Society (ACS) ,1971