The Functionally Distinct Hemoglobins of the Arctic Spotted Wolffish Anarhichas minor
The Arctic fish Anarhichas minor, a benthic sedentary species, displays high hemoglobin multiplicity. The three major hemoglobins (Hb 1, Hb 2, and Hb 3) show important functional differences in pH and organophosphate regulation, subunit cooperativity, and response of oxygen binding to temperature. H...
Published in: | Journal of Biological Chemistry |
---|---|
Main Authors: | , , , , , |
Format: | Article in Journal/Newspaper |
Language: | English |
Published: |
2002
|
Subjects: | |
Online Access: | https://www.openaccessrepository.it/record/94653 https://doi.org/10.1074/jbc.m202474200 |
id |
ftopenaccessrep:oai:zenodo.org:94653 |
---|---|
record_format |
openpolar |
spelling |
ftopenaccessrep:oai:zenodo.org:94653 2023-10-25T01:32:22+02:00 The Functionally Distinct Hemoglobins of the Arctic Spotted Wolffish Anarhichas minor Elio Parisi Antonio Riccio Maurizio Tamburrini Cinzia Verde Guido di Prisco Vito Carratore 2002-07-16 https://www.openaccessrepository.it/record/94653 https://doi.org/10.1074/jbc.m202474200 eng eng url:https://www.openaccessrepository.it/communities/itmirror https://www.openaccessrepository.it/record/94653 doi:10.1074/jbc.m202474200 info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by/4.0/ Cell Biology Molecular Biology Biochemistry info:eu-repo/semantics/article publication-article 2002 ftopenaccessrep https://doi.org/10.1074/jbc.m202474200 2023-09-26T22:21:07Z The Arctic fish Anarhichas minor, a benthic sedentary species, displays high hemoglobin multiplicity. The three major hemoglobins (Hb 1, Hb 2, and Hb 3) show important functional differences in pH and organophosphate regulation, subunit cooperativity, and response of oxygen binding to temperature. Hb 1 and Hb 2 display a low, effector-enhanced Bohr effect and no Root effect. In contrast, Hb 3 displays pronounced Bohr and Root effects, accompanied by strong organophosphate regulation. Hb 1 has the beta (beta(1)) chain in common with Hb 2; Hb 3 and Hb 2 share the alpha (alpha(2)) chain. The amino acid sequences have been established. Several substitutions in crucial positions were observed, such as Cys in place of C-terminal His in the beta(1) chain of Hb 1 and Hb 2. In Hb 3, Val E11 of the beta(2) chain is replaced by Ile. Homology modeling revealed an unusual structure of the Hb 3 binding site of inositol hexakisphoshate. Phylogenetic analysis indicated that only Hb 2 displays higher overall similarity with the major Antarctic hemoglobins. The oxygen transport system of A. minor differs remarkably from those of Antarctic Notothenioidei, indicating distinct evolutionary pathways in the regulatory mechanisms of the fish respiratory system in the two polar environments. Article in Journal/Newspaper Antarc* Antarctic Arctic Istituto Nazionale di Fisica Nucleare (INFN): Open Access Repository Antarctic Arctic Journal of Biological Chemistry 277 39 36312 36320 |
institution |
Open Polar |
collection |
Istituto Nazionale di Fisica Nucleare (INFN): Open Access Repository |
op_collection_id |
ftopenaccessrep |
language |
English |
topic |
Cell Biology Molecular Biology Biochemistry |
spellingShingle |
Cell Biology Molecular Biology Biochemistry Elio Parisi Antonio Riccio Maurizio Tamburrini Cinzia Verde Guido di Prisco Vito Carratore The Functionally Distinct Hemoglobins of the Arctic Spotted Wolffish Anarhichas minor |
topic_facet |
Cell Biology Molecular Biology Biochemistry |
description |
The Arctic fish Anarhichas minor, a benthic sedentary species, displays high hemoglobin multiplicity. The three major hemoglobins (Hb 1, Hb 2, and Hb 3) show important functional differences in pH and organophosphate regulation, subunit cooperativity, and response of oxygen binding to temperature. Hb 1 and Hb 2 display a low, effector-enhanced Bohr effect and no Root effect. In contrast, Hb 3 displays pronounced Bohr and Root effects, accompanied by strong organophosphate regulation. Hb 1 has the beta (beta(1)) chain in common with Hb 2; Hb 3 and Hb 2 share the alpha (alpha(2)) chain. The amino acid sequences have been established. Several substitutions in crucial positions were observed, such as Cys in place of C-terminal His in the beta(1) chain of Hb 1 and Hb 2. In Hb 3, Val E11 of the beta(2) chain is replaced by Ile. Homology modeling revealed an unusual structure of the Hb 3 binding site of inositol hexakisphoshate. Phylogenetic analysis indicated that only Hb 2 displays higher overall similarity with the major Antarctic hemoglobins. The oxygen transport system of A. minor differs remarkably from those of Antarctic Notothenioidei, indicating distinct evolutionary pathways in the regulatory mechanisms of the fish respiratory system in the two polar environments. |
format |
Article in Journal/Newspaper |
author |
Elio Parisi Antonio Riccio Maurizio Tamburrini Cinzia Verde Guido di Prisco Vito Carratore |
author_facet |
Elio Parisi Antonio Riccio Maurizio Tamburrini Cinzia Verde Guido di Prisco Vito Carratore |
author_sort |
Elio Parisi |
title |
The Functionally Distinct Hemoglobins of the Arctic Spotted Wolffish Anarhichas minor |
title_short |
The Functionally Distinct Hemoglobins of the Arctic Spotted Wolffish Anarhichas minor |
title_full |
The Functionally Distinct Hemoglobins of the Arctic Spotted Wolffish Anarhichas minor |
title_fullStr |
The Functionally Distinct Hemoglobins of the Arctic Spotted Wolffish Anarhichas minor |
title_full_unstemmed |
The Functionally Distinct Hemoglobins of the Arctic Spotted Wolffish Anarhichas minor |
title_sort |
functionally distinct hemoglobins of the arctic spotted wolffish anarhichas minor |
publishDate |
2002 |
url |
https://www.openaccessrepository.it/record/94653 https://doi.org/10.1074/jbc.m202474200 |
geographic |
Antarctic Arctic |
geographic_facet |
Antarctic Arctic |
genre |
Antarc* Antarctic Arctic |
genre_facet |
Antarc* Antarctic Arctic |
op_relation |
url:https://www.openaccessrepository.it/communities/itmirror https://www.openaccessrepository.it/record/94653 doi:10.1074/jbc.m202474200 |
op_rights |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by/4.0/ |
op_doi |
https://doi.org/10.1074/jbc.m202474200 |
container_title |
Journal of Biological Chemistry |
container_volume |
277 |
container_issue |
39 |
container_start_page |
36312 |
op_container_end_page |
36320 |
_version_ |
1780728043019436032 |