Occurrence and formation of endogenous histidine hexa‐coordination in cold‐adapted hemoglobins
Abstract Spectroscopic and crystallographic evidence of endogenous (His) ligation at the sixth coordination site of the heme iron has been reported for monomeric, dimeric, and tetrameric hemoglobins (Hbs) in both ferrous (hemochrome) and ferric (hemichrome) oxidation states. In particular, the ferri...
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crwiley:10.1002/iub.446 2024-06-02T07:58:20+00:00 Occurrence and formation of endogenous histidine hexa‐coordination in cold‐adapted hemoglobins Merlino, Antonello Howes, Barry D. Prisco, Guido di Verde, Cinzia Smulevich, Giulietta Mazzarella, Lelio Vergara, Alessandro 2011 http://dx.doi.org/10.1002/iub.446 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fiub.446 https://iubmb.onlinelibrary.wiley.com/doi/pdf/10.1002/iub.446 en eng Wiley http://onlinelibrary.wiley.com/termsAndConditions#vor IUBMB Life volume 63, issue 5, page 295-303 ISSN 1521-6543 1521-6551 journal-article 2011 crwiley https://doi.org/10.1002/iub.446 2024-05-03T11:31:12Z Abstract Spectroscopic and crystallographic evidence of endogenous (His) ligation at the sixth coordination site of the heme iron has been reported for monomeric, dimeric, and tetrameric hemoglobins (Hbs) in both ferrous (hemochrome) and ferric (hemichrome) oxidation states. In particular, the ferric bis‐ histidyl adduct represents a common accessible ordered state for the β chains of all tetrameric Hbs isolated from Antarctic and sub‐Antarctic fish. Indeed, the crystal structures of known tetrameric Hbs in the bis‐His state are characterized by a different binding state of the α and β chains. An overall analysis of the bis‐histidyl adduct of globin structures deposited in the Protein Data Bank reveals a marked difference between hemichromes in tetrameric Hbs compared to monomeric/dimeric Hbs. Herein, we review the structural, spectroscopic and stability features of hemichromes in tetrameric Antarctic fish Hbs. The role of bis‐histidyl adducts is also addressed in a more evolutionary context alongside the concept of its potential physiological role. © 2011 IUBMB IUBMB Life, 63(5): 295–303, 2011 Article in Journal/Newspaper Antarc* Antarctic Wiley Online Library Antarctic IUBMB Life 63 5 295 303 |
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Wiley Online Library |
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crwiley |
language |
English |
description |
Abstract Spectroscopic and crystallographic evidence of endogenous (His) ligation at the sixth coordination site of the heme iron has been reported for monomeric, dimeric, and tetrameric hemoglobins (Hbs) in both ferrous (hemochrome) and ferric (hemichrome) oxidation states. In particular, the ferric bis‐ histidyl adduct represents a common accessible ordered state for the β chains of all tetrameric Hbs isolated from Antarctic and sub‐Antarctic fish. Indeed, the crystal structures of known tetrameric Hbs in the bis‐His state are characterized by a different binding state of the α and β chains. An overall analysis of the bis‐histidyl adduct of globin structures deposited in the Protein Data Bank reveals a marked difference between hemichromes in tetrameric Hbs compared to monomeric/dimeric Hbs. Herein, we review the structural, spectroscopic and stability features of hemichromes in tetrameric Antarctic fish Hbs. The role of bis‐histidyl adducts is also addressed in a more evolutionary context alongside the concept of its potential physiological role. © 2011 IUBMB IUBMB Life, 63(5): 295–303, 2011 |
format |
Article in Journal/Newspaper |
author |
Merlino, Antonello Howes, Barry D. Prisco, Guido di Verde, Cinzia Smulevich, Giulietta Mazzarella, Lelio Vergara, Alessandro |
spellingShingle |
Merlino, Antonello Howes, Barry D. Prisco, Guido di Verde, Cinzia Smulevich, Giulietta Mazzarella, Lelio Vergara, Alessandro Occurrence and formation of endogenous histidine hexa‐coordination in cold‐adapted hemoglobins |
author_facet |
Merlino, Antonello Howes, Barry D. Prisco, Guido di Verde, Cinzia Smulevich, Giulietta Mazzarella, Lelio Vergara, Alessandro |
author_sort |
Merlino, Antonello |
title |
Occurrence and formation of endogenous histidine hexa‐coordination in cold‐adapted hemoglobins |
title_short |
Occurrence and formation of endogenous histidine hexa‐coordination in cold‐adapted hemoglobins |
title_full |
Occurrence and formation of endogenous histidine hexa‐coordination in cold‐adapted hemoglobins |
title_fullStr |
Occurrence and formation of endogenous histidine hexa‐coordination in cold‐adapted hemoglobins |
title_full_unstemmed |
Occurrence and formation of endogenous histidine hexa‐coordination in cold‐adapted hemoglobins |
title_sort |
occurrence and formation of endogenous histidine hexa‐coordination in cold‐adapted hemoglobins |
publisher |
Wiley |
publishDate |
2011 |
url |
http://dx.doi.org/10.1002/iub.446 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fiub.446 https://iubmb.onlinelibrary.wiley.com/doi/pdf/10.1002/iub.446 |
geographic |
Antarctic |
geographic_facet |
Antarctic |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_source |
IUBMB Life volume 63, issue 5, page 295-303 ISSN 1521-6543 1521-6551 |
op_rights |
http://onlinelibrary.wiley.com/termsAndConditions#vor |
op_doi |
https://doi.org/10.1002/iub.446 |
container_title |
IUBMB Life |
container_volume |
63 |
container_issue |
5 |
container_start_page |
295 |
op_container_end_page |
303 |
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1800741649807048704 |