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Crystal structure of rat heme oxygenase-1 in complex with heme
FEBS Letters, 2000 Heme oxygenase catalyzes the oxidative cleavage of protoheme to biliverdin, the first step of heme metabolism utilizing O2 and NADPH. We determined the crystal structures of rat heme oxygenase-1 (HO-1)–heme and selenomethionyl HO-1–heme complexes.
Masakazu Sugishima +2 more
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Heme oxygenase-1 and heme oxygenase-2 expression in bruises
Forensic Science, Medicine, and Pathology, 2015The 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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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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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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The mechanism of heme oxygenase
Current Opinion in Chemical Biology, 2000Major advances have been made in determining the structure of heme oxygenase and the relationship between its structure and catalytic activity. The nature of the first step in the reaction sequence, heme alpha-meso-hydroxylation, is now clear, although the mechanisms that control the alpha-regiospecificity remain elusive. Hypothetical mechanisms can be
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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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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 in the retina in diabetes
Current Eye Research, 2003Heme oxygenase (HO) isoforms, HO-1, and HO-2, are responsible for heme breakdown to iron and carbon monoxide (CO). HO may respond to oxidative stress and may modulate the expression of vasoactive factors like nitric oxide (NO). Since diabetes induced oxidative stress may change HO, the present study examined whether diabetes is associated with HO ...
Mark, Cukiernik +3 more
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Heme oxygenase and renal disease
Current Hypertension Reports, 2009The cellular content of heme, derived from the breakdown of heme proteins, is regulated via the heme oxygenase (HO) enzyme system. HO catalyzes the rate-limiting step in heme degradation resulting in the formation of iron, carbon monoxide, and biliverdin.
Tambi, Jarmi, Anupam, Agarwal
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Expression of Heme Oxygenase in Hemopoiesis
1988Heme oxygenase has been purified to electrophoretic homogeneity from detergent solubilized adult human liver microsomes. Treatment of microsomes with Triton X-100, sodium cholate and subsequent batchwise DEAE-cellulose, 2', 5' ADP-sepharose 4B, Sepharose CLB and hydroxylapatite column resulted in 17% yield of the purified heme oxygenase.
Nader G. Abraham +5 more
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Current Pharmaceutical Design, 2008
Heme oxygenase-1 (HO-1) is an inducible rate-limiting enzyme which catalyzes group heme into carbon monoxide, iron and bilirubin. In the recent years, HO-1 expression has been reported as an important protective endogenous mechanism against physical, chemical and biological stress.
FERRÁNDIZ, M.L., Devesa Giner, Isabel
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Heme oxygenase-1 (HO-1) is an inducible rate-limiting enzyme which catalyzes group heme into carbon monoxide, iron and bilirubin. In the recent years, HO-1 expression has been reported as an important protective endogenous mechanism against physical, chemical and biological stress.
FERRÁNDIZ, M.L., Devesa Giner, Isabel
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Different Faces of the Heme-Heme Oxygenase System in Inflammation
Pharmacological Reviews, 2003The heme-heme oxygenase system has recently been recognized to possess important regulatory properties. It is tightly involved in both physiological as well as pathophysiological processes, such as cytoprotection, apoptosis, and inflammation. Heme functions as a double-edged sword.
Wagener, F.A.D.T.G. +6 more
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