ArticleDrug metabolism and disposition: the biological fate of chemicals2009
Measurement of membrane-bound human heme oxygenase-1 activity using a chemically defined assay system.
Article in Drug metabolism and disposition: the biological fate of chemicals, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 25 citations in OpenAlex.
- Bottom-Up Model Suggesting Membrane Localization of Heme Oxygenase‑1 Contributes to Heme Selection for Degradation.ACS omega · 2026Article
- Heme and CO metabolism by the canonical human heme oxygenases.Journal of inorganic biochemistry · 2026Review
- Heteromeric complex formation between human cytochrome P450 CYP1A1 and heme oxygenase-1.The Biochemical journal · 2021Article
- Activation of artemisinin and heme degradation in Leishmania tarentolae promastigotes: A possible link.Biochemical pharmacology · 2020Article
- Recent Advances in the Understanding of the Reaction Chemistries of the Heme Catabolizing Enzymes HO and BVR Based on High Resolution Protein Structures.Current medicinal chemistry · 2020Review
- Instability of the Human Cytochrome P450 Reductase A287P Variant Is the Major Contributor to Its Antley-Bixler Syndrome-like Phenotype.The Journal of biological chemistry · 2016Article
- Beneficial effects of diminished production of hydrogen sulfide or carbon monoxide on hypertension and renal injury induced by NO withdrawal.British journal of pharmacology · 2015Article
- Protein/protein interactions in the mammalian heme degradation pathway: heme oxygenase-2, cytochrome P450 reductase, and biliverdin reductase.The Journal of biological chemistry · 2014Article
- Structural insights into human heme oxygenase-1 inhibition by potent and selective azole-based compounds.Journal of the Royal Society, Interface · 2013Article
- Article
- Mutations of human cytochrome P450 reductase differentially modulate heme oxygenase-1 activity and oligomerization.Archives of biochemistry and biophysics · 2011Article
- Inhibition of cytochrome P450 1A2-mediated metabolism and production of reactive oxygen species by heme oxygenase-1 in rat liver microsomes.Drug metabolism letters · 2011Article
- Human heme oxygenase-1 efficiently catabolizes heme in the absence of biliverdin reductase.Drug metabolism and disposition: the biological fate of chemicals · 2010Article
- Human cytochrome P450 oxidoreductase deficiency caused by the Y181D mutation: molecular consequences and rescue of defect.Drug metabolism and disposition: the biological fate of chemicals · 2010Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Heme oxygenase (HO) catalyzes heme degradation in a reaction requiring NADPH-cytochrome P450 reductase (CPR). Although most studies with HO used a soluble 30-kDa form, lacking the C-terminal membrane-binding region, recent reports show that the catalytic behavior of this enzyme is very different if this domain is retained; the overall activity was elevated 5-fold, and the K(m) for CPR decreased approximately 50-fold. The goal of these studies was to accurately measure HO activity using a coupled assay containing purified biliverdin reductase (BVR). This allows measurement of bilirubin formation after incorporation of full-length CPR and heme oxygenase-1 (HO-1) into a membrane environment. When rat liver cytosol was used as the source of partially purified BVR, the reaction remained linear for 2 to 3 min; however, the reaction was only linear for 10 to 30 s when an equivalent amount of purified, human BVR (hBVR) was used. This lack of linearity was not observed with soluble HO-1. Optimal formation of bilirubin was achieved with concentrations of bovine serum albumin (0.25 mg/ml) and hBVR (0.025-0.05 microM), but neither supplement increased the time that the reaction remained linear. Various concentrations of superoxide dismutase had no effect on the reaction; however, when catalase was included, the reactions were linear for at least 4 to 5 min, even at high CPR levels. These results not only show that HO-1-generated hydrogen peroxide leads to a decrease in HO-1 activity but also provide for a chemically defined system to be used to examine the function of full-length HO-1 in a membrane environment.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.