title: Purification and characterization of the single-component nitric oxide reductase from Ralstonia eutropha H16.
abstract: Nitric oxide (NO) reductase was purified from Ralstonia eutropha (formerly Alcaligenes eutrophus) using a two step chromatographic procedure. Unlike the common NO reductases, the enzyme consists of a single subunit of 75 kDa which contains both high-spin and low-spin heme b, but lacks heme c. One additional iron atom, probably a ferric non-heme iron, was identified per enzyme molecule. Whereas reduced cytochrome c was ineffective as electron donor, NO was reduced at a specific activity of 2.3 micromol/min per mg of protein in the presence of 2-methyl-1,4-naphthoquinol.
authors.affiliation: Institut für Biologie/Mikrobiologie, Humboldt-Universität zu Berlin, Germany. rainer.cramm@rz.hu-berlin.de
authors.forename: R
authors.initials: R
authors.lastname: Cramm
authors.forename: A
authors.initials: A
authors.lastname: Pohlmann
authors.forename: B
authors.initials: B
authors.lastname: Friedrich
mesh_terms: D001205:Ascorbic Acid / Q000737:chemistry; D001426:Bacterial Proteins / Q000737:chemistry; D020118:Cupriavidus necator / Q000201:enzymology*; D004578:Electron Spin Resonance Spectroscopy; D004579:Electron Transport; D004591:Electrophoresis, Polyacrylamide Gel; D006418:Heme / Q000737:chemistry; D006420:Hemeproteins / Q000737:chemistry; D007501:Iron / Q000737:chemistry; D007700:Kinetics; D008773:Methylphenazonium Methosulfate / Q000737:chemistry; D010088:Oxidoreductases / Q000737:chemistry*; D013053:Spectrophotometry; D013772:Tetramethylphenylenediamine / Q000737:chemistry; D014812:Vitamin K / Q000737:chemistry
chemical_list: D001426:Bacterial Proteins; D006420:Hemeproteins; D014812:Vitamin K; D008773:Methylphenazonium Methosulfate; D006418:Heme; D007501:Iron; D010088:Oxidoreductases; C034747:nitric-oxide reductase; D013772:Tetramethylphenylenediamine; D001205:Ascorbic Acid