Characterization of organic matter in a sediment Core near the Mataripe refinery, Bahia-Brazil.

A sediment core was taken from the Todos os Santos Bay, near the Mataripe Bahia-Brazil refinery. The results of dating, (210)Pb and (137)Cs methods, combined with organic indicators, Polycyclic aromatic hydrocarbons (PAHs), n-alkanes and total organic carbon (TOC), showed significant change with the start of production of the oil fields of Aratu, Itaparica and Dom João (1939-1947) and the construction of the Mataripe refinery (1949-1950). This event was marked by a series of significant changes, including an abrupt increase in TOC and the growth of PAH concentrations and the presence Unresolved/Resolved ratio (UR/R)>4 in n-alkanes fraction, which indicated that the contamination was of petrogenic origin. The δ(13)C of specific n-alkanes compounds showed gradual deplete with the depth.

Changes in the spin state and reactivity of cytochrome C induced by photochemically generated singlet oxygen and free radicals.

This work compares the effect of photogenerated singlet oxygen (O(2)((1)Delta(g))) (type II mechanism) and free radicals (type I mechanism) on cytochrome c structure and reactivity. Both reactive species were obtained by photoexcitation of methylene blue (MB(+)) in the monomer and dimer forms, respectively. The monomer form is predominant at low dye concentrations (up to 8 microm) or in the presence of an excess of SDS micelles, while dimers are predominant at 0.7 mm SDS. Over a pH range in which cytochrome c is in the native form, O(2) ((1)Delta(g)) and free radicals induced a Soret band blue shift (from 409 to 405 nm), predominantly. EPR measurements revealed that the blue shift of the Soret band was compatible with conversion of the heme iron from its native low spin state to a high spin state with axial symmetry (g approximately 6.0). Soret band bleaching, due to direct attack on the heme group, was only detected under conditions that favored free radical production (MB(+) dimer in SDS micelles) or in the presence of a less structured form of the protein (above pH 9.3). Matrix-assisted laser desorption ionization time-of-flight mass spectrometry of the heme group and the polypeptide chain of cytochrome c with Soret band at 405 nm (cytc405) revealed no alterations in the mass of the cytc405 heme group but oxidative modifications on methionine (Met(65) and Met(80)) and tyrosine (Tyr(74)) residues. Damage of cytc405 tyrosine residue impaired its reduction by diphenylacetaldehyde, but not by beta-mercaptoethanol, which was able to reduce cytc405, generating cytochrome c Fe(II) in the high spin state (spin 2).