SAXS structure of homodimeric oxyHemoglobin III from bivalve Lucina pectinata.
Amino Acid Sequence
Animals
Bivalvia
/ genetics
Crystallography, X-Ray
Electrophoresis, Polyacrylamide Gel
Heme
/ chemistry
Hydrogen Sulfide
/ metabolism
Oxyhemoglobins
/ chemistry
Protein Conformation
Protein Multimerization
Scattering, Small Angle
Sequence Homology, Amino Acid
Tandem Mass Spectrometry
/ methods
X-Ray Diffraction
/ methods
SAXS
hemeproteins
protein oligomerization
Journal
Biopolymers
ISSN: 1097-0282
Titre abrégé: Biopolymers
Pays: United States
ID NLM: 0372525
Informations de publication
Date de publication:
Jun 2021
Jun 2021
Historique:
revised:
07
03
2021
received:
31
08
2020
accepted:
10
03
2021
pubmed:
2
4
2021
medline:
15
12
2021
entrez:
1
4
2021
Statut:
ppublish
Résumé
Hemoglobin III (HbIII) is one of the two oxygen reactive hemoproteins present in the bivalve, Lucina pectinata. The clam inhabits a sulfur-rich environment and HbIII is the only hemoprotein present in the system which does not yet have a structure described elsewhere. It is known that HbIII exists as a heterodimer with hemoglobin II (HbII) to generate the stable Oxy(HbII-HbIII) complex but it remains unknown if HbIII can form a homodimeric species. Here, a new chromatographic methodology to separate OxyHbIII from the HbII-HbIII dimer has been developed, employing a fast performance liquid chromatography and ionic exchange chromatography column. The nature of OxyHbIII in solution at concentrations from 1.6 mg/mL to 20.4 mg/mL was studied using small angle X-ray scattering (SAXS). The results show that at all concentrations, the Oxy(HbIII-HbIII) dimer dominates in solution. However, as the concentration increases to nonphysiological values, 20.4 mg/mL, HbIII forms a 30% tetrameric fraction. Thus, there is a direct relationship between the Oxy(HbIII-HbIII) oligomeric form and hemoglobin concentration. We suggest it is likely that the OxyHbIII dimer contributes to active oxygen transport in tissues of L pectinata, where the Oxy(HbII-HbIII) complex is not present.
Identifiants
pubmed: 33792032
doi: 10.1002/bip.23427
pmc: PMC8265735
mid: NIHMS1716551
doi:
Substances chimiques
Oxyhemoglobins
0
Heme
42VZT0U6YR
Hydrogen Sulfide
YY9FVM7NSN
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
e23427Subventions
Organisme : NIGMS NIH HHS
ID : P20 GM103475
Pays : United States
Organisme : BioXFEL Science and Technology Center
ID : STC-1231306
Organisme : Alfred P Sloan Minority PhD Program
ID : 2010-3-02
Organisme : NIH INBRE PR
ID : P20GM103475
Informations de copyright
© 2021 Wiley Periodicals LLC.
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