Amino acid sequence of the cooperative homodimeric hemoglobin from the mollusc Scapharca inaequivalvis and topology of the intersubunit contacts

FEBS Letters

Barra, Donatella¹  Bossa, Francesco¹  Petruzzelli, Raffaele¹  Chiancone, Emilia¹  Verzili, Daniela¹  Boffi, Alberto¹  Goffredo, Bianca M.¹  Ascoli, Franca² 

[1] CNR Center of Molecular Biology, Institute of Biochemistry, University of Rome ‘La Sapienza’, Piazzale de Aldo Moro 5, 00185 RomeItaly;Department of Cell Biology, University of Camerino, 62032 Camerino (Mc, Italy

关键词: Molluscan hemoglobin Amino acid sequence Hemoglobin assembly;   

DOI  :  10.1016/0014-5793(85)80632-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The dimeric hemoglobin (HbI) from Scapharca inaequivalvis is highly homologous to the other known dimeric Arcid hemoglobins. The sequence has a distinctive hydrophobicity profile in the region corresponding to the E and F helices with respect to both the hemoglobin and myoglobin chains from vertebrates due to the presence of several additional hydrophobic residues. The characteristic topology of the E and F helices is conserved in all the known sequences of Arcid hemoglobins including that of the so-called α chain of the tetrameric component from Anadara trapezia. The rationale for this conservation lies in the unusual assembly of Arcid hemoglobins where the E and F helices are involved in the interdimeric contact. It is suggested that the extra hydrophobic residues play a major role in the assembly of the basic dimeric unit in these hemoglobins.

【 授权许可】

Unknown