ArticleBiochemical and biophysical research communications2008
Mass spectrometric identification of lysine residues of heme oxygenase-1 that are involved in its interaction with NADPH-cytochrome P450 reductase.
Article in Biochemical and biophysical research communications, 2008. 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, 15 citations in OpenAlex.
- Heme and CO metabolism by the canonical human heme oxygenases.Journal of inorganic biochemistry · 2026Review
- 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
- Identification of danthron as an isoform-specific inhibitor of HEME OXYGENASE-1/cytochrome P450 reductase interaction with anti-tumor activity.Journal of biomedical science · 2018Article
- Amino Acid Insertion Frequencies Arising from Photoproducts Generated Using Aliphatic Diazirines.Journal of the American Society for Mass Spectrometry · 2017Article
- Translocation of heme oxygenase-1 contributes to imatinib resistance in chronic myelogenous leukemia.Oncotarget · 2017Article
- Protein/protein interactions in the mammalian heme degradation pathway: heme oxygenase-2, cytochrome P450 reductase, and biliverdin reductase.The Journal of biological chemistry · 2014Article
- New insights into intracellular locations and functions of heme oxygenase-1.Antioxidants & redox signaling · 2014Review
- Structural basis for the electron transfer from an open form of NADPH-cytochrome P450 oxidoreductase to heme oxygenase.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Dynamic control of electron transfers in diflavin reductases.International journal of molecular sciences · 2012Review
- Article
- Human heme oxygenase-1 efficiently catabolizes heme in the absence of biliverdin reductase.Drug metabolism and disposition: the biological fate of chemicals · 2010Article
- Oligomerization is crucial for the stability and function of heme oxygenase-1 in the endoplasmic reticulum.The Journal of biological chemistry · 2009Article
- C-Terminal membrane spanning region of human heme oxygenase-1 mediates a time-dependent complex formation with cytochrome P450 reductase.Biochemistry · 2009Article
- Probing protein structure by amino acid-specific covalent labeling and mass spectrometry.Mass spectrometry reviewsReview
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
Abstract
The lysine residues of rat heme oxygenase-1 (HO-1) were acetylated by acetic anhydride in the absence and presence of NADPH-cytochrome P450 reductase (CPR) or biliverdin reductase (BVR). Nine acetylated peptides were identified by MALDI-TOF mass spectrometry in the tryptic fragments obtained from HO-1 acetylated without the reductases (referred to as the fully acetylated HO-1). The presence of CPR prevented HO-1 from acetylation of lysine residues, Lys-149 and Lys-153, located in the F-helix. The heme degradation activity of the fully acetylated HO-1 in the NADPH/CPR-supported system was significantly reduced, whereas almost no inactivation was detected in HO-1 in the presence of CPR, which prevented acetylation of Lys-149 and Lys-153. On the other hand, the presence of BVR showed no protective effect on the acetylation of HO-1. The interaction of HO-1 with CPR or BVR is discussed based on the acetylation pattern and on molecular modeling.
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