Structural characterization of the Oxidation pathway of Antarctic fish hemoglobin
Antarctic fish hemoglobins (AF-Hbs) exhibit a peculiar oxidation process. Our previous crystallographic and spectroscopic investigations have demonstrated that, upon oxidation, these proteins show a remarkable propensity to evolve toward the formation of lowspin hexa-coordinated species. The crystal...
Main Authors: | , , , , , , , |
---|---|
Other Authors: | , , , , , , , |
Format: | Article in Journal/Newspaper |
Language: | English |
Published: |
2005
|
Subjects: | |
Online Access: | http://hdl.handle.net/11588/307720 http://journals.iucr.org/a/issues/2005/a1/00/issconts.html |
id |
ftunivnapoliiris:oai:www.iris.unina.it:11588/307720 |
---|---|
record_format |
openpolar |
spelling |
ftunivnapoliiris:oai:www.iris.unina.it:11588/307720 2024-06-23T07:47:22+00:00 Structural characterization of the Oxidation pathway of Antarctic fish hemoglobin L. Vitagliano G. Bonomi M. Franzese C. Verde G. di Prisco MERLINO, ANTONELLO VERGARA, ALESSANDRO MAZZARELLA, LELIO L., Vitagliano G., Bonomi M., Franzese Merlino, Antonello Vergara, Alessandro C., Verde G., di Prisco Mazzarella, Lelio 2005 STAMPA http://hdl.handle.net/11588/307720 http://journals.iucr.org/a/issues/2005/a1/00/issconts.html eng eng volume:61 firstpage:C215 lastpage:C215 numberofpages:1 journal:ACTA CRYSTALLOGRAPHICA. SECTION A, FOUNDATIONS OF CRYSTALLOGRAPHY http://hdl.handle.net/11588/307720 http://journals.iucr.org/a/issues/2005/a1/00/issconts.html hemoglobin protein oxidation protein cooperativity info:eu-repo/semantics/article 2005 ftunivnapoliiris 2024-06-03T14:30:13Z Antarctic fish hemoglobins (AF-Hbs) exhibit a peculiar oxidation process. Our previous crystallographic and spectroscopic investigations have demonstrated that, upon oxidation, these proteins show a remarkable propensity to evolve toward the formation of lowspin hexa-coordinated species. The crystal structures of the fully oxidized forms of AF-Hbs, isolated from Trematomus newnesi and Trematomus bernacchii, have also shown that and chains follow different oxidation pathways. Interestingly, the quaternary structures of these forms are intermediate between the physiological R and T hemoglobin states. In order to obtain additional information on the structural features of the intermediate species along the oxidation pathway, we are currently characterizing AF-Hbs exposed to air for different time periods. Preliminary data reveal the presence of novel forms with unexpected structural properties. In particular, we detected (1)the presence of partially liganded forms with structures that are intermediate between the R and the T state, (2) the existence of hybrid alpha(aquomet)-beta(penta-coordinated Fe3+) forms, and (3) the occurrence of novel subunit-subunit interactions at the alpha 1beta2 interface. Article in Journal/Newspaper Antarc* Antarctic IRIS Università degli Studi di Napoli Federico II Antarctic |
institution |
Open Polar |
collection |
IRIS Università degli Studi di Napoli Federico II |
op_collection_id |
ftunivnapoliiris |
language |
English |
topic |
hemoglobin protein oxidation protein cooperativity |
spellingShingle |
hemoglobin protein oxidation protein cooperativity L. Vitagliano G. Bonomi M. Franzese C. Verde G. di Prisco MERLINO, ANTONELLO VERGARA, ALESSANDRO MAZZARELLA, LELIO Structural characterization of the Oxidation pathway of Antarctic fish hemoglobin |
topic_facet |
hemoglobin protein oxidation protein cooperativity |
description |
Antarctic fish hemoglobins (AF-Hbs) exhibit a peculiar oxidation process. Our previous crystallographic and spectroscopic investigations have demonstrated that, upon oxidation, these proteins show a remarkable propensity to evolve toward the formation of lowspin hexa-coordinated species. The crystal structures of the fully oxidized forms of AF-Hbs, isolated from Trematomus newnesi and Trematomus bernacchii, have also shown that and chains follow different oxidation pathways. Interestingly, the quaternary structures of these forms are intermediate between the physiological R and T hemoglobin states. In order to obtain additional information on the structural features of the intermediate species along the oxidation pathway, we are currently characterizing AF-Hbs exposed to air for different time periods. Preliminary data reveal the presence of novel forms with unexpected structural properties. In particular, we detected (1)the presence of partially liganded forms with structures that are intermediate between the R and the T state, (2) the existence of hybrid alpha(aquomet)-beta(penta-coordinated Fe3+) forms, and (3) the occurrence of novel subunit-subunit interactions at the alpha 1beta2 interface. |
author2 |
L., Vitagliano G., Bonomi M., Franzese Merlino, Antonello Vergara, Alessandro C., Verde G., di Prisco Mazzarella, Lelio |
format |
Article in Journal/Newspaper |
author |
L. Vitagliano G. Bonomi M. Franzese C. Verde G. di Prisco MERLINO, ANTONELLO VERGARA, ALESSANDRO MAZZARELLA, LELIO |
author_facet |
L. Vitagliano G. Bonomi M. Franzese C. Verde G. di Prisco MERLINO, ANTONELLO VERGARA, ALESSANDRO MAZZARELLA, LELIO |
author_sort |
L. Vitagliano |
title |
Structural characterization of the Oxidation pathway of Antarctic fish hemoglobin |
title_short |
Structural characterization of the Oxidation pathway of Antarctic fish hemoglobin |
title_full |
Structural characterization of the Oxidation pathway of Antarctic fish hemoglobin |
title_fullStr |
Structural characterization of the Oxidation pathway of Antarctic fish hemoglobin |
title_full_unstemmed |
Structural characterization of the Oxidation pathway of Antarctic fish hemoglobin |
title_sort |
structural characterization of the oxidation pathway of antarctic fish hemoglobin |
publishDate |
2005 |
url |
http://hdl.handle.net/11588/307720 http://journals.iucr.org/a/issues/2005/a1/00/issconts.html |
geographic |
Antarctic |
geographic_facet |
Antarctic |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_relation |
volume:61 firstpage:C215 lastpage:C215 numberofpages:1 journal:ACTA CRYSTALLOGRAPHICA. SECTION A, FOUNDATIONS OF CRYSTALLOGRAPHY http://hdl.handle.net/11588/307720 http://journals.iucr.org/a/issues/2005/a1/00/issconts.html |
_version_ |
1802651465721839616 |