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Heme-Oxygenase-1

Antioxidants & Redox Signaling, 2020
This Forum issue "Heme Oxygenase" (HO) includes original research articles and reviews that are aimed at understanding the role of HO-1 in several pathophysiological conditions, specially addressing those involving inflammation and oxidative damage. Overall, the seven contributions of this Forum highlight the dual role that HO-1 displays in cells and ...
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Heme oxygenase and heme degradation

Biochemical and Biophysical Research Communications, 2005
The microsomal heme oxygenase system consists of heme oxygenase (HO) and NADPH-cytochrome P450 reductase, and plays a key role in the physiological catabolism of heme which yields biliverdin, carbon monoxide, and iron as the final products. Heme degradation proceeds essentially as a series of autocatalytic oxidation reactions involving heme bound to HO.
Goro, Kikuchi   +2 more
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Non-heme iron oxygenases

Current Opinion in Chemical Biology, 2002
Our understanding of the biological significance and chemical properties of non-heme iron oxygenases has increased dramatically in recent years. New group members have emerged from genome sequences and biochemical analyses. Spectroscopic and crystallographic studies have provided critical insights into catalysis.
Matthew J, Ryle, Robert P, Hausinger
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Heme oxygenase-1 and heme oxygenase-2 expression in bruises

Forensic Science, Medicine, and Pathology, 2015
The first step in catabolism of hemoglobin in a bruise is performed by the enzyme heme oxygenase, which produces biliverdin that is then reduced to bilirubin. The development of yellow coloration in bruises can be attributed to local accumulation of degradation products of hemoglobin, including bilirubin, but it is not clear why there is a delay before
Neil E I, Langlois   +3 more
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Mechanism of heme degradation by heme oxygenase

Journal of Inorganic Biochemistry, 2000
Heme oxygenase catalyzes the three step-wise oxidation of hemin to alpha-biliverdin, via alpha-meso-hydroxyhemin, verdoheme, and ferric iron-biliverdin complex. This enzyme is a simple protein which does not have any prosthetic groups. However, heme and its two metabolites, alpha-meso-hydroxyhemin and verdoheme, combine with the enzyme and activate ...
T, Yoshida, C T, Migita
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Heme Oxygenase-1

American Journal of Respiratory Cell and Molecular Biology, 2002
Oxidative stresses such as oxidant stimuli, inflammation, exposure to xenobiotics, and ionizing irradiation elicit various tissue injuries and provoke cellular responses, principally involving transcriptional activation of genes encoding proteins which participate in the defense reactions (Camhi et al., 1995).
Toru Takahashi   +4 more
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Bacterial Heme Oxygenases

Antioxidants & Redox Signaling, 2004
The importance of heme oxygenases in heme catabolism, iron utilization, and cellular signaling has been recognized for many years and is a well studied process in eukaryotes. Through the accessibility of an increasing number of bacterial genomes, it has become evident that heme oxygenases are also widespread in prokaryotes. In these organisms, the heme
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