High Resolution Crystal Structures of the Cerebratulus lacteus Mini-Hb in the Unligated and Carbomonoxy States

International Journal of Molecular Sciences

Francesca Germani¹  Alessandra Pesce³  Andrea Venturini³  Luc Moens¹  Martino Bolognesi²  Sylvia Dewilde¹ 

[1] Department of Biomedical Sciences, University of Antwerp, Universiteitsplein 1, B-2610 Antwerp, Belgium; E-Mails:;Dipartimento di BioScienze, Università degli Studi di Milano, Via Celoria 26, I-20133 Milano, Italy; E-Mail:;Department of Physics, University of Genova, Via Dodecaneso 33, I-16146 Genova, Italy; E-Mails:

关键词: nerve globin;    crystal structure;    heme reactivity;    carbon monoxide;    protein matrix tunnel;   

DOI  :  10.3390/ijms13078025

来源: mdpi

【 摘 要 】

The nerve tissue mini-hemoglobin from Cerebratulus lacteus (CerHb) displays an essential globin fold hosting a protein matrix tunnel held to allow traffic of small ligands to and from the heme. CerHb heme pocket hosts the distal TyrB10/GlnE7 pair, normally linked to low rates of O₂ dissociation and ultra-high O₂ affinity. However, CerHb affinity for O₂ is similar to that of mammalian myoglobins, due to a dynamic equilibrium between high and low affinity states driven by the ability of ThrE11 to orient the TyrB10 OH group relative to the heme ligand. We present here the high resolution crystal structures of CerHb in the unligated and carbomonoxy states. Although CO binds to the heme with an orientation different from the O₂ ligand, the overall binding schemes for CO and O₂ are essentially the same, both ligands being stabilized through a network of hydrogen bonds based on TyrB10, GlnE7, and ThrE11. No dramatic protein structural changes are needed to support binding of the ligands, which can freely reach the heme distal site through the apolar tunnel. A lack of main conformational changes between the heme-unligated and -ligated states grants stability to the folded mini-Hb and is a prerequisite for fast ligand diffusion to/from the heme.

【 授权许可】

CC BY   
© 2012 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland.