Results 251 to 260 of about 115,890 (298)
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DNA and Cell Biology, 2002
Heme plays a significant pathogenic role in several diseases involving the kidney. The cellular content of heme, derived either from the delivery of filtered heme proteins such as hemoglobin and myoglobin, or from the breakdown of ubiquitous intracellular heme proteins, is regulated via the heme oxygenase enzyme system.
Nathalie, Hill-Kapturczak +2 more
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Heme plays a significant pathogenic role in several diseases involving the kidney. The cellular content of heme, derived either from the delivery of filtered heme proteins such as hemoglobin and myoglobin, or from the breakdown of ubiquitous intracellular heme proteins, is regulated via the heme oxygenase enzyme system.
Nathalie, Hill-Kapturczak +2 more
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Mechanism of heme degradation by heme oxygenase
Journal of Inorganic Biochemistry, 2000Heme 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 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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Crystal structure of rat heme oxygenase-1 in complex with heme [PDF]
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.
Yoshimitsu Kakuta, Masakazu Sugishima
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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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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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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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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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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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