Issue 49, 2014

Structural modifications induced by the switch from an endogenous bis-histidyl to an exogenous cyanomet hexa-coordination in a tetrameric haemoglobin

Abstract

Ferric cold-adapted fish haemoglobins exhibit heterogeneous coordination at the α (aquo-met) and β (bis-histidyl) subunits. Herein we report two EPR-distinct bis-histidyl conformers (I and II) of the β subunits of ferric haemoglobin from Trematomus bernacchii which react differently with CN. An EPR titration reveals that upon cyanidation the most distorted conformer I reacts faster than II, producing both a cyanided and penta-coordinate ferric forms in the β subunits. The X-ray crystal structure of the partially cyanided conformer I reveals both an order-disorder transition and details of a communication between α and β subunits.

Graphical abstract: Structural modifications induced by the switch from an endogenous bis-histidyl to an exogenous cyanomet hexa-coordination in a tetrameric haemoglobin

Supplementary files

Article information

Article type
Paper
Submitted
12 Apr 2014
Accepted
29 May 2014
First published
04 Jun 2014

RSC Adv., 2014,4, 25852-25856

Author version available

Structural modifications induced by the switch from an endogenous bis-histidyl to an exogenous cyanomet hexa-coordination in a tetrameric haemoglobin

L. Mazzarella, A. Merlino, L. Vitagliano, C. Verde, G. di Prisco, J. Peisach and A. Vergara, RSC Adv., 2014, 4, 25852 DOI: 10.1039/C4RA03317E

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