Deciphering the structural role of histidine 83 for heme binding in hemophore HasA
Heme carrier HasA has a unique type of histidine/tyrosine heme iron ligation in which the
iron ion is in a thermally driven two spin states equilibrium. We recently suggested that the H-
bonding between Tyr 75 and the invariantly conserved residue His 83 modulates the
strength of the iron-Tyr 75 bond. To unravel the role of His 83, we characterize the iron
ligation and the electronic properties of both wild type and H83A mutant by a variety of
spectroscopic techniques. Although His 83 in wild type modulates the strength of the Tyr-iron …
iron ion is in a thermally driven two spin states equilibrium. We recently suggested that the H-
bonding between Tyr 75 and the invariantly conserved residue His 83 modulates the
strength of the iron-Tyr 75 bond. To unravel the role of His 83, we characterize the iron
ligation and the electronic properties of both wild type and H83A mutant by a variety of
spectroscopic techniques. Although His 83 in wild type modulates the strength of the Tyr-iron …
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