Abstract
The binding of NO to the iron heme in guanylate cyclase and other heme proteins induces the cleavage of the proximal histidine bonded to the metal. In this study we assess by means of density functional theory (DFT) electronic structure calculations the role of H-bonding to histidine in the modulation of this effect. We have considered in the first place a model of the isolated active site coordinated with imidazole and imidazolate to mimic the effects of a very strong H-bond. We have also investigated four selected ferrous heme proteins with different proximal histidine environments: the O2 sensing FixL, horseradish peroxidase C, and the α and β subunits of human hemoglobin. Our results indicate that polarization and charge transfer effects associated with H-bonding to the proximal histidine play a fundamental role in the modulation of the NO trans effect in heme proteins. We also find computational evidence suggesting that protein structural constraints may affect significantly the cleavage of the Fe-His bond.
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Acknowledgements
D.A.E. and F.D. acknowledge partial financial support from Fundación Antorchas, Universidad de Buenos Aires, ANPCYT, and the L.B.P. Endowment for the Sciences and Arts. D.A.E. acknowledges Pablo de Grande and Microsoft Argentina for a generous donation. D.A.E. and F.D. are members of CONICET (Argentina). P.O. acknowledges support from Spain Fundación Ramón Areces and McyT. M.A.M. acknowledges A. Turjanski, A. Crespo, M. González Lebrero, and V. Lenz for valuable discussions.
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Martí, M.A., Scherlis, D.A., Doctorovich, F.A. et al. Modulation of the NO trans effect in heme proteins: implications for the activation of soluble guanylate cyclase. J Biol Inorg Chem 8, 595–600 (2003). https://doi.org/10.1007/s00775-003-0452-9
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DOI: https://doi.org/10.1007/s00775-003-0452-9