Ct. Allocatelli et al., ENGINEERING ASCARIS HEMOGLOBIN OXYGEN-AFFINITY IN SPERM WHALE MYOGLOBIN - ROLE OF TYROSINE B10, FEBS letters, 352(1), 1994, pp. 63-66
The contribution to oxygen stabilization of a tyrosine residue in topo
logical position (B10) has been studied in sperm whale myoglobin by si
multaneous replacement of residues at positions (B10), (E7) and (E10)
as suggested by analysis of the sequence of high oxygen affinity hemog
lobins, such as that of the nematode Ascaris suum. Kinetic and equilib
rium experiments with the gaseous ligands oxygen and carbon monoxide s
how that indeed the introduction of tyrosine (B10), together with repl
acement of the distal histidine (E7) with glutamine, is associated wit
h a large decrease in the oxygen dissociation rate constant. Our resul
ts are consistent with the possible formation in the distal pocket of
two hydrogen bonds with the iron-bound oxygen.