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PDBsum entry 6iyh
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Oxygen binding/transport protein
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PDB id
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6iyh
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References listed in PDB file
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Key reference
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Title
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Novel X-Ray sequences and crystal structures of persian and starry sturgeon methemoglobins: highlighting the role of heme pocket waters in causing autoxidation.
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Authors
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A.Seyedarabi,
S.Ariaeenejad,
A.A.Moosavi-Movahedi,
S.Rayati,
N.Poursasan,
N.Asiaie,
Z.Seraj,
F.Mehraban,
S.E.Seyedarabi.
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Ref.
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Biochim Biophys Acta Proteins Proteom, 2019,
1867,
586-594.
[DOI no: ]
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PubMed id
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Note: In the PDB file this reference is
annotated as "TO BE PUBLISHED". The citation details given above have
been manually determined.
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Abstract
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Although there is a high sequence similarity between mammalian and fish
hemoglobin (Hb), the oxidation and heme loss rates can vary greatly between them
such that fish Hbs oxidise much more rapidly than mammalian Hbs. There is to
date no sequence or structural data for any sturgeon Hb to reveal the level of
autoxidation in these fish. In this study, novel high resolution X-ray sequences
and crystal structures of methemoglobin (Met-Hb) from two sturgeon fish
including Persian sturgeon (Acipenser percisus) and Starry sturgeon (Acipenser
stellatus) belonging to the Caspian sea has been determined. A comprehensive
sequence and structure comparison between these sturgeon Met-Hbs and a number of
non-sturgeon and normal and sickle cell anaemia human Hb in varying heme states
has been carried out highlighting (i) the structural variability in the heme
propionate groups; (ii) the existence of certain residues or their displacement
and shift in the heme pocket allowing entry of water molecules into the heme
pocket; (iii) the importance of the number of water molecules in the heme
pocket; (iv) the hydrogen bonding between oxygens of A and D propionate groups
and that of waters in the heme pocket; and (v) the role of heme binding waters
causing oxidative stress and heme autoxidation.
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