TAILIEUCHUNG - Báo cáo khoa học: The oxidation process of Antarctic fish hemoglobins

Analysis of the molecular properties of proteins extracted from organisms living under extreme conditions often highlights peculiar features. We investigated by UV-visible spectroscopy and X-ray crystallography the oxidation pro-cess, promoted by air or ferricyanide, of five hemoglobins extracted from Antarctic fishes (Notothenioidei). | Eur. J. Biochem. 271 1651-1659 2004 FEBS 2004 doi The oxidation process of Antarctic fish hemoglobins Luigi Vitagliano1 I Giovanna Bonomi2 I Antonio Riccio3 Guido di Prisco3 Giulietta Smulevich4 and Lelio Mazzarella1 2 1Istituto di Biostrutture e Bioimmagini CNR Napoli 2Dipartimento di Chimica Universita degli Studi di Napoli Federico II Complesso Universitario di . Angelo Napoli 3Istituto di Biochimica delle Proteine CNR Napoli Italy 4Dipartimento di Chimica Universiia degli Studi di Firenze Polo Scientifico Sesto Fiorentino Italy Analysis of the molecular properties of proteins extracted from organisms living under extreme conditions often highlights peculiar features. We investigated by UV-visible spectroscopy and X-ray crystallography the oxidation process promoted by air or ferricyanide of five hemoglobins extracted from Antarctic fishes Notothenioidei . Spectroscopic analysis revealed that these hemoglobins share a common oxidation pathway which shows striking differences from the oxidation processes of hemoglobins from other vertebrates. Indeed simple exposure of these hemoglobins to air leads to the formation of a significant amount of the low-spin hexacoordinated form denoted hemichrome. This hemichrome form which is detected under a variety of experimental conditions can be reversibly transformed to either carbomonoxy or deoxygenated forms with reducing agents. Interestingly the spectra of the fully oxidized species obtained by treating the protein with ferricyanide show the simultaneous presence of peaks corresponding to different hexacoordinated states the aquomet and the hemichrome. In order to assign the heme region state of the a and b chains the air-oxidized and ferricyanide-oxidized forms of Trematomus bernacchii hemoglobin were crystallized. Crystallographic analysis revealed that these forms correspond to an a aquomet -b bishistidyl-hemichrome state. This demonstrates that the a and b chains of Antarctic fish .

• Báo cáo khoa học
• Report medicine
• traditional medicine
• scientific reports
• Crystal structure
• medical analysis
• biochemical studies
• medical knowledge
• medical research
• analysis of cytoplasmic
• oxidation
• bacteria
• hemoglobin
• medicine
• cell proliferation
• breast cancer
• chemical reaction
• gastric cancer
• hormone medicine
• tumor cells
• environmental medicine