How does NO activate hemeproteins?
- 21 March 1994
- journal article
- review article
- Published by Wiley in FEBS Letters
- Vol. 341 (2-3), 141-145
- https://doi.org/10.1016/0014-5793(94)80445-1
Abstract
NO was reported to activate guanylate cyclase and, recently, prostaglandin H synthase. NO interaction with the heme component in different hemeproteins is determined by ligand property, electronic configuration of the heme iron and the specific effects contributed by the protein structure. It is found that although NO interaction with the free heme provides some common rules of interaction, the consequences of NO binding to different hemeproteins should be dealt with individually.Keywords
This publication has 17 references indexed in Scilit:
- Photochemistry of nitric oxide adducts of water-soluble iron(III) porphyrin and ferrihemoproteins studied by nanosecond laser photolysisJournal of the American Chemical Society, 1993
- Conversion of Nitroxyl (HNO) to Nitric Oxide (NO) in Biological Systems: The Role of Physiological Oxidants and Relevance to the Biological Activity of HNOBiochemical and Biophysical Research Communications, 1993
- Reversible Binding of Nitric Oxide by a Salivary Heme Protein from a Bloodsucking InsectScience, 1993
- Nitric oxide-triggered heme-mediated hydrolysis: a possible model for biological reactions of NOJournal of the American Chemical Society, 1993
- Why nitric oxide?Biochemistry, 1992
- Nitric oxide, an inhibitor of lipid oxidation by lipoxygenase, cyclooxygenase and hemoglobinLipids, 1992
- [34] Purification of heme-containing soluble guanylyl cyclaseMethods in Enzymology, 1991
- Reaction of nitric oxide with heme proteins and model compounds of hemoglobinBiochemistry, 1987
- Nitric oxide ferrohemes: kinetics of formation and photodissociation quantum yieldsJournal of the American Chemical Society, 1983
- Soluble guanylate cyclase purified from bovine lung contains heme and copperFEBS Letters, 1981