1s5y
From Proteopedia
(New page: 200px<br /> <applet load="1s5y" size="450" color="white" frame="true" align="right" spinBox="true" caption="1s5y, resolution 2.50Å" /> '''The crystal structu...) |
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caption="1s5y, resolution 2.50Å" /> | caption="1s5y, resolution 2.50Å" /> | ||
'''The crystal structure of Trematomus bernacchii hemoglobin oxidized by ferricyanide'''<br /> | '''The crystal structure of Trematomus bernacchii hemoglobin oxidized by ferricyanide'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1S5Y is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Trematomus_bernacchii Trematomus bernacchii] with ACE and HEM as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1S5Y is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Trematomus_bernacchii Trematomus bernacchii] with <scene name='pdbligand=ACE:'>ACE</scene> and <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S5Y OCA]. |
==Reference== | ==Reference== | ||
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[[Category: oxidation]] | [[Category: oxidation]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:52:25 2008'' |
Revision as of 14:52, 15 February 2008
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The crystal structure of Trematomus bernacchii hemoglobin oxidized by ferricyanide
Overview
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 alpha, and beta chains, the air-oxidized and ferricyanide-oxidized forms of, Trematomus bernacchii hemoglobin were crystallized. Crystallographic, analysis revealed that these forms correspond to an, alpha(aquomet)-beta(bishistidyl-hemichrome) state. This demonstrates that, the alpha and beta chains of Antarctic fish hemoglobins follow very, different oxidation pathways. As found for Trematomus newnesi hemoglobin, in a partial hemichrome state [Riccio, A., Vitagliano, L., di Prisco, G., Zagari, A. & Mazzarella, L. (2002) Proc. Natl Acad. Sci. USA99, 9801-9806], the quaternary structures of these, alpha(aquomet)-beta(bishistidyl-hemichrome) forms are intermediate between, the physiological R and T hemoglobin states. Together, these structures, provide information on the general features of this intermediate state.
About this Structure
1S5Y is a Protein complex structure of sequences from Trematomus bernacchii with and as ligands. Full crystallographic information is available from OCA.
Reference
The oxidation process of Antarctic fish hemoglobins., Vitagliano L, Bonomi G, Riccio A, di Prisco G, Smulevich G, Mazzarella L, Eur J Biochem. 2004 May;271(9):1651-9. PMID:15096204
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