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Deciphering the structural role of histidine 83 for heme binding in hemophore HasA.

Abstract : 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 Tyr75 and the invariantly conserved residue His83 modulates the strength of the iron-Tyr75 bond. To unravel the role of His83, we characterize the iron ligation and the electronic properties of both wild type and H83A mutant by a variety of spectroscopic techniques. Although His83 in wild type modulates the strength of the Tyr-iron bond, its removal causes detachment of the tyrosine ligand, thus giving rise to a series of pH-dependent equilibria among species with different axial ligation. The five coordinated species detected at physiological pH may represent a possible intermediate of the heme transfer mechanism to the receptor.
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Submitted on : Tuesday, March 3, 2009 - 2:17:20 PM
Last modification on : Thursday, April 7, 2022 - 10:10:19 AM
Long-term archiving on: : Saturday, November 26, 2016 - 6:18:10 AM

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Célia Caillet-Saguy, Paola Turano, Mario Piccioli, Gudrun S. Lukat-Rodgers, Mirjam Czjzek, et al.. Deciphering the structural role of histidine 83 for heme binding in hemophore HasA.. Journal of Biological Chemistry, 2008, 283 (9), pp.5960-70. ⟨10.1074/jbc.M703795200⟩. ⟨pasteur-00365415⟩

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