title: How the atmosphere and the presence of substrate affect the photo and non-photoinactivation of heme enzymes by uroporphyrin I.
abstract: 1. The effect of URO I on the activity of ALA-D, PBGase, deaminase and URO-D, both in aerobiosis and anaerobiosis, was studied. 2. Photoinactivation of the enzymes was much lower in an anaerobic than in an aerobic atmosphere. 3. Dark inactivation in the absence of oxygen was lower than its presence. 4. Preincubation in the presence of ALA or PBG protected the enzymic activity of ALA-D, PBGase and deaminase against URO I-inactivation both under u.v. light and in the dark. 5. Photoinactivating action of URO I would be mediated by reactive oxygen species generated by the excited porphyrin after its absorption of light. Dark inactivation, in aerobiosis, can also be partly mediated by amino acid oxidation, although to a lesser extent than that observed under u.v. light.
authors.affiliation: Centro de Investigaciones sobre Porfirinas y Porfirias (CIPYP), University of Buenos Aires, Argentina.
authors.forename: S G
authors.initials: SG
authors.lastname: Afonso
authors.forename: S
authors.initials: S
authors.lastname: Chinarro
authors.forename: R
authors.initials: R
authors.lastname: Enriquez de Salamanca
authors.forename: A M
authors.initials: AM
authors.lastname: Batlle
mesh_terms: D000332:Aerobiosis; D000642:Ammonia-Lyases / Q000037:antagonists & inhibitors; D000693:Anaerobiosis; D003624:Darkness; D004791:Enzyme Inhibitors / Q000494:pharmacology*; D006801:Humans; D011163:Hydroxymethylbilane Synthase / Q000037:antagonists & inhibitors; D008027:Light; D000623:Porphobilinogen Synthase / Q000037:antagonists & inhibitors; D014575:Uroporphyrinogen Decarboxylase / Q000037:antagonists & inhibitors; D014578:Uroporphyrins / Q000494:pharmacology*
chemical_list: D004791:Enzyme Inhibitors; D014578:Uroporphyrins; C034103:uroporphyrin I; D011163:Hydroxymethylbilane Synthase; D014575:Uroporphyrinogen Decarboxylase; D000623:Porphobilinogen Synthase; D000642:Ammonia-Lyases; C100132:porphobilinogenase