title: Novel detection method of nitric oxide using horseradish peroxidase.
abstract: Nitric oxide (NO) readily makes corresponding complexes not only with ferrous iron but also with ferric iron. However, NO-ferric complexes of many heme proteins were unstable, while horseradish peroxidase formed the very stable NO-ferric porphyrin complex with a shift of the Soret band of the absorption wavelength from 396.5 nm to 420.0 nm. The concentration of NO in aqueous media could be monitored by measuring the absorption changes, and the detection limit was 10 nM. The simple procedure is convenient for concentration determination of NO solution.
authors.affiliation: Faculty of Pharmaceutical Sciences, University of Tokyo, Japan.
authors.forename: K
authors.initials: K
authors.lastname: Kikuchi
authors.forename: T
authors.initials: T
authors.lastname: Nagano
authors.forename: M
authors.initials: M
authors.lastname: Hirobe
mesh_terms: D002138:Calibration; D005290:Ferric Compounds / Q000378:metabolism; D006420:Hemeproteins / Q000378:metabolism; D006735:Horseradish Peroxidase / Q000378:metabolism*; D009569:Nitric Oxide / Q000032:analysis*; D013053:Spectrophotometry
chemical_list: D005290:Ferric Compounds; D006420:Hemeproteins; D009569:Nitric Oxide; D006735:Horseradish Peroxidase