Scapharca hemoglobins, type cases of a novel mode of chain assembly and heme-heme communication. Amino acid sequence and subunit interactions of the tetrameric component.
The sequences of the A and B chains of the Scapharca inaequivalvis tetrameric hemoglobin (HbII) are reported. They are homologous to the corresponding chains of other Arcid hemoglobins. Moreover, a comparison of the present data with the sequence of the S. inaequivalvis dimeric hemoglobin (HbI), for which high-resolution X-ray data are available, allows the identification of the residues that direct the assembly of the two components and of those that may be involved in the interdimeric contacts.
Petruzzelli
R
R
Department of Biochemical Sciences, University La Sapienza, Rome, Italy.
Boffi
A
A
Barra
D
D
Bossa
F
F
Ascoli
F
F
Chiancone
E
E
D000494:Allosteric Regulation; D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D006418:Heme; D006454:Hemoglobins / Q000235:genetics* / Q000648:ultrastructure; D008969:Molecular Sequence Data; D008974:Mollusca / Q000502:physiology*; D011485:Protein Binding; D013329:Structure-Activity Relationship
D006454:Hemoglobins; D006418:Heme