1s5y

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{{STRUCTURE_1s5y| PDB=1s5y | SCENE= }}
{{STRUCTURE_1s5y| PDB=1s5y | SCENE= }}
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'''The crystal structure of Trematomus bernacchii hemoglobin oxidized by ferricyanide'''
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===The crystal structure of Trematomus bernacchii hemoglobin oxidized by ferricyanide===
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==Overview==
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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. &amp; 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.
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{{ABSTRACT_PUBMED_15096204}}
==About this Structure==
==About this Structure==
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==Reference==
==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:[http://www.ncbi.nlm.nih.gov/pubmed/15096204 15096204]
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:[http://www.ncbi.nlm.nih.gov/pubmed/15096204 15096204]
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The crystal structure of a tetrameric hemoglobin in a partial hemichrome state., Riccio A, Vitagliano L, di Prisco G, Zagari A, Mazzarella L, Proc Natl Acad Sci U S A. 2002 Jul 23;99(15):9801-6. Epub 2002 Jul 1. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12093902 12093902]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Trematomus bernacchii]]
[[Category: Trematomus bernacchii]]
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[[Category: Hemichrome]]
[[Category: Hemichrome]]
[[Category: Oxidation]]
[[Category: Oxidation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:20:35 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 04:42:17 2008''

Revision as of 01:42, 29 July 2008

Image:1s5y.png

Template:STRUCTURE 1s5y

The crystal structure of Trematomus bernacchii hemoglobin oxidized by ferricyanide

Template:ABSTRACT PUBMED 15096204

About this Structure

1S5Y is a Protein complex structure of sequences from Trematomus bernacchii. 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

The crystal structure of a tetrameric hemoglobin in a partial hemichrome state., Riccio A, Vitagliano L, di Prisco G, Zagari A, Mazzarella L, Proc Natl Acad Sci U S A. 2002 Jul 23;99(15):9801-6. Epub 2002 Jul 1. PMID:12093902

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