Scapharca inaequivalvis Hemoglobins: Novel Cooperative Assemblies of Globin Chains (original) (raw)

Structure and Function of Invertebrate Oxygen Carriers, 1991

Abstract

The crystal structures of the Hbs from the clam Scapharca inaequivalvis (Hbl, a homodimer, and Hbll, a heterotetramer) (1-3), and from the “fat innkeeper” worm Urechis caupo (a homotetramer) (4) have revealed novel assemblages of Mb-folded chains that differ markedly from that characteristic of the α2β2 vertebrate Hb tetramer (5).

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