Root effect also functions modulating the hemichrome stability in tetrameric hemoglobins
Oxidation of hemoglobins leads to the formation of Fe(III) forms, whose relevance spans from biochemical to physiological aspects 1. Here we report a combined EPR/X-ray crystallography study at acidic pH on six ferric tetrameric hemoglobins (Hbs), five isolated from the Antarctic fish species Tremat...
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ftunivnapoliiris:oai:www.iris.unina.it:11588/346249 2024-06-23T07:47:23+00:00 Root effect also functions modulating the hemichrome stability in tetrameric hemoglobins VERGARA, ALESSANDRO FRANZESE, MARISA MERLINO, ANTONELLO BONOMI, GIOVANNA MAZZARELLA, LELIO C. Verde D. Giordano G. Di Prisco C. Lee J. Peisach Vergara, Alessandro Franzese, Marisa Merlino, Antonello Bonomi, Giovanna C., Verde D., Giordano G., Di Prisco C., Lee J., Peisach Mazzarella, Lelio 2008 STAMPA http://hdl.handle.net/11588/346249 http://www.chimica.unige.it/37cncf/index.htm eng eng country:ITA place:Genova ispartofbook:XXXVII Congresso nazionale di Chimica Fisica XXXVII Congresso nazionale di Chimica Fisica firstpage:21 lastpage:21 http://hdl.handle.net/11588/346249 http://www.chimica.unige.it/37cncf/index.htm info:eu-repo/semantics/conferencePaper 2008 ftunivnapoliiris 2024-06-10T14:58:47Z Oxidation of hemoglobins leads to the formation of Fe(III) forms, whose relevance spans from biochemical to physiological aspects 1. Here we report a combined EPR/X-ray crystallography study at acidic pH on six ferric tetrameric hemoglobins (Hbs), five isolated from the Antarctic fish species Trematomus bernacchii, Trematomus newnesi, and Gymnodraco acuticeps, and one from the sub-Antarctic fish Cottoperca gobio. Our data reveal that, in all the studied Hbs, aquomet form and two hemichromes coexist at acidic pH, analogously to what happens at physiological pH 2. Nevertheless, the EPR analysis reveals that, only for the three Root effect hemoglobins 3,4, a significant amount of pentacoordinated (5C) high-spin Fe(III) species appears at acidic pH. The crystal structure at acidic pH of the ferric hemoglobin from Trematomus bernacchii, endowed with Root effect 4, is also reported at 1.7 Å. Indeed, this structure reveals a 5C state both at α- and β-chains within a T-like quaternary structure. The ability of the Antarctic fish Hbs to form 5C states in various conditions prompted us to perform a peroxidase activity study. These proteins exhibit a peroxidase activity higher than that observed for mammalian and temperate fish Hbs , thus suggesting that a partial hemichrome state in tetrameric Hbs does not protect them from peroxidation as previously proposed 5. This work was financially supported by PNRA (Italian National Programme for Antarctic Research) 1 A. Vergara, L. Vitagliano, G. di Prisco, C. Verde, and L. Mazzarella, Meth. Enz. 436A, 421 (2008). 2 A. Vergara, M. Franzese, A. Merlino, L. Vitagliano, G. di Prisco, C. Verde, H. C. Lee, J. Peisach, and L. Mazzarella, Biophys. J. 93, 2822 (2007). 3 L. Mazzarella, G. Bonomi, M. C. Lubrano, A. Merlino, A. Vergara, L. Vitagliano, C. Verde, and G. di Prisco, Proteins: Struct. Funct. Bioinf. 62, 316 (2006). 4 L. Mazzarella, A. Vergara, L. Vitagliano, A. Merlino, G. Bonomi, S. Scala, C. Verde, and G. di Prisco, Proteins: Struct. Funct. Bioinf. 65, 490 (2006). 5 L. Feng, ... Conference Object Antarc* Antarctic IRIS Università degli Studi di Napoli Federico II Antarctic The Antarctic |
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IRIS Università degli Studi di Napoli Federico II |
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ftunivnapoliiris |
language |
English |
description |
Oxidation of hemoglobins leads to the formation of Fe(III) forms, whose relevance spans from biochemical to physiological aspects 1. Here we report a combined EPR/X-ray crystallography study at acidic pH on six ferric tetrameric hemoglobins (Hbs), five isolated from the Antarctic fish species Trematomus bernacchii, Trematomus newnesi, and Gymnodraco acuticeps, and one from the sub-Antarctic fish Cottoperca gobio. Our data reveal that, in all the studied Hbs, aquomet form and two hemichromes coexist at acidic pH, analogously to what happens at physiological pH 2. Nevertheless, the EPR analysis reveals that, only for the three Root effect hemoglobins 3,4, a significant amount of pentacoordinated (5C) high-spin Fe(III) species appears at acidic pH. The crystal structure at acidic pH of the ferric hemoglobin from Trematomus bernacchii, endowed with Root effect 4, is also reported at 1.7 Å. Indeed, this structure reveals a 5C state both at α- and β-chains within a T-like quaternary structure. The ability of the Antarctic fish Hbs to form 5C states in various conditions prompted us to perform a peroxidase activity study. These proteins exhibit a peroxidase activity higher than that observed for mammalian and temperate fish Hbs , thus suggesting that a partial hemichrome state in tetrameric Hbs does not protect them from peroxidation as previously proposed 5. This work was financially supported by PNRA (Italian National Programme for Antarctic Research) 1 A. Vergara, L. Vitagliano, G. di Prisco, C. Verde, and L. Mazzarella, Meth. Enz. 436A, 421 (2008). 2 A. Vergara, M. Franzese, A. Merlino, L. Vitagliano, G. di Prisco, C. Verde, H. C. Lee, J. Peisach, and L. Mazzarella, Biophys. J. 93, 2822 (2007). 3 L. Mazzarella, G. Bonomi, M. C. Lubrano, A. Merlino, A. Vergara, L. Vitagliano, C. Verde, and G. di Prisco, Proteins: Struct. Funct. Bioinf. 62, 316 (2006). 4 L. Mazzarella, A. Vergara, L. Vitagliano, A. Merlino, G. Bonomi, S. Scala, C. Verde, and G. di Prisco, Proteins: Struct. Funct. Bioinf. 65, 490 (2006). 5 L. Feng, ... |
author2 |
Vergara, Alessandro Franzese, Marisa Merlino, Antonello Bonomi, Giovanna C., Verde D., Giordano G., Di Prisco C., Lee J., Peisach Mazzarella, Lelio |
format |
Conference Object |
author |
VERGARA, ALESSANDRO FRANZESE, MARISA MERLINO, ANTONELLO BONOMI, GIOVANNA MAZZARELLA, LELIO C. Verde D. Giordano G. Di Prisco C. Lee J. Peisach |
spellingShingle |
VERGARA, ALESSANDRO FRANZESE, MARISA MERLINO, ANTONELLO BONOMI, GIOVANNA MAZZARELLA, LELIO C. Verde D. Giordano G. Di Prisco C. Lee J. Peisach Root effect also functions modulating the hemichrome stability in tetrameric hemoglobins |
author_facet |
VERGARA, ALESSANDRO FRANZESE, MARISA MERLINO, ANTONELLO BONOMI, GIOVANNA MAZZARELLA, LELIO C. Verde D. Giordano G. Di Prisco C. Lee J. Peisach |
author_sort |
VERGARA, ALESSANDRO |
title |
Root effect also functions modulating the hemichrome stability in tetrameric hemoglobins |
title_short |
Root effect also functions modulating the hemichrome stability in tetrameric hemoglobins |
title_full |
Root effect also functions modulating the hemichrome stability in tetrameric hemoglobins |
title_fullStr |
Root effect also functions modulating the hemichrome stability in tetrameric hemoglobins |
title_full_unstemmed |
Root effect also functions modulating the hemichrome stability in tetrameric hemoglobins |
title_sort |
root effect also functions modulating the hemichrome stability in tetrameric hemoglobins |
publisher |
country:ITA |
publishDate |
2008 |
url |
http://hdl.handle.net/11588/346249 http://www.chimica.unige.it/37cncf/index.htm |
geographic |
Antarctic The Antarctic |
geographic_facet |
Antarctic The Antarctic |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_relation |
ispartofbook:XXXVII Congresso nazionale di Chimica Fisica XXXVII Congresso nazionale di Chimica Fisica firstpage:21 lastpage:21 http://hdl.handle.net/11588/346249 http://www.chimica.unige.it/37cncf/index.htm |
_version_ |
1802651483629420544 |