Biochimica et Biophysica Acta (BBA) - General Subjects
Functional consequences of ligand-linked dissociation in hemoglobin from the sea cucumber molpadia arenicola
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Cited by (18)
Diversity of coelomocytes in the class Holothuroidea
2023, The World of Sea Cucumbers: Challenges, Advances, and InnovationsTertiary and quaternary effects in the allosteric regulation of animal hemoglobins
2013, Biochimica et Biophysica Acta - Proteins and ProteomicsCitation Excerpt :The single globin types are insensitive to organic phosphates, but bind oxygen with a measurable cooperativity, that is enhanced when the D globin is added to any of the others [148]. It has been suggested that cooperative oxygen binding arises from assemblage of dimers, upon deoxygenation, into low-affinity tetramers and higher aggregates [149]. Interestingly, the subunit interface of homodimeric Caudina Hb-D closely resembles that of S. inaequivalvis HbI, mainly formed by residues from the E and F helices, and involving the heme propionates.
Allosteric hemoglobin assembly: Diversity and similarity
2005, Journal of Biological ChemistryCitation Excerpt :Isolated EF dimeric hemoglobins have been observed in the mollusc, Scapharca inaequivalvis (20), and the echinoderm, Caudina arenicola (21). The Scapharca HbI homodimer shows significant cooperative ligand binding (22), whereas strong cooperativity requires heterodimeric forms of Caudina hemoglobin (21, 23). S. inaequivalvis also possesses a cooperative tetrameric hemoglobin, which is assembled from two EF heterodimers (24) (Fig. 2).
Nonvertebrate hemoglobins: Structural bases for reactivity
1997, Progress in Biophysics and Molecular BiologyStructural Analysis of Monomeric Hemichrome and Dimeric Cyanomet Hemoglobins fromCaudina arenicola
1995, Journal of Molecular BiologyAmino acid sequence of a globin from the sea cucumber Caudina (Molpadia) arenicola
1991, Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular