ArticleJournal of the American Chemical Society2009
Characterization of the proximal ligand in the P420 form of inducible nitric oxide synthase.
Article in Journal of the American Chemical Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 32 citations in OpenAlex.
- Xenobiotic-Metabolizing Enzymes in Trematodes.Biomedicines · 2022Review
- Domain-Swap Dimerization ofMolecular pharmacology · 2020Article
- A nitric oxide synthase-like protein fromThe Journal of biological chemistry · 2019Article
- Endogenous insertion of non-native metalloporphyrins into human membrane cytochrome P450 enzymes.The Journal of biological chemistry · 2018Article
- Spectroscopic evidence supporting neutral thiol ligation to ferrous heme iron.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018Article
- Importance of Val567 on heme environment and substrate recognition of neuronal nitric oxide synthase.FEBS open bio · 2018Article
- Redox-dependent stability, protonation, and reactivity of cysteine-bound heme proteins.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Investigations of heme ligation and ligand switching in cytochromes p450 and p420.Biochemistry · 2013Article
- Experimental documentation of the structural consequences of hydrogen-bonding interactions to the proximal cysteine of a cytochrome P450.Angewandte Chemie (International ed. in English) · 2012Article
- Article
- Rational engineering of cytochromes P450 2B6 and 2B11 for enhanced stability: Insights into structural importance of residue 334.Archives of biochemistry and biophysics · 2010Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The nitric oxide (NO) produced by inducible nitric oxide synthase (iNOS) up-regulates the expression of heme oxygenase (HO), which in turn produces carbon monoxide (CO) that down-regulates iNOS activity by reducing its expression level or by inhibiting its activity by converting it to an inactive P420 form (iNOS(P420)). Accordingly, CO has been considered as a potentially important attenuator of inflammation. Despite its importance, the nature of the proximal heme ligand of the iNOS(P420) species remains elusive. Here we show that the 221 cm(-1) mode of the photoproduct of iNOS(P420) does not exhibit any H(2)O-D(2)O solvent isotope shift such as that found in the iron-histidine stretching mode of myoglobin, indicating that the proximal ligand of iNOS(P420) is not a histidine. The nu(Fe-CO) and nu(C-O) data reveal that the proximal heme ligand of iNOS(P420) is consistent with a protonated thiol instead of a thiolate anion. Furthermore, the optical absorption properties of iNOS(P420) are similar to those of a neutral thiol-heme model complex but not myoglobin. Together the data support the scenario that iNOS(P420) is inactivated by protonation of the native proximal thiolate ligand to a neutral thiol, instead of by ligand switching to a histidine, as prior studies have suggested.
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