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Tension in haemoglobin revealed by Fe-His(F8) bond rupture in the fully liganded T-state.
J Mol Biol 1997; 271(2):161-7JM

Abstract

In 1972, Perutz proposed that the low affinity of T-state haemoglobin is caused by tension in the bond between the iron and the proximal histidine, restraining the Fe from moving into the porphyrin plane on binding oxygen. This proposal has often been disputed. If such tension does exist, it will be manifest in the liganded T-state. Here we describe the structure of the fully liganded T-state cyanide complex of haemoglobin, in which the Fe-proximal histidine bond in the alpha-subunits, but not in the beta-subunits, is ruptured. This rupture uncouples the structural changes at the alpha-haem from those in the globin and the beta-haem, and demonstrates unequivocally the existence of tension and its transmission through this bond.

Authors+Show Affiliations

Department of Chemistry, University of York, York, YO1 5DD, UK.No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

9268649

Citation

Paoli, M, et al. "Tension in Haemoglobin Revealed By Fe-His(F8) Bond Rupture in the Fully Liganded T-state." Journal of Molecular Biology, vol. 271, no. 2, 1997, pp. 161-7.
Paoli M, Dodson G, Liddington RC, et al. Tension in haemoglobin revealed by Fe-His(F8) bond rupture in the fully liganded T-state. J Mol Biol. 1997;271(2):161-7.
Paoli, M., Dodson, G., Liddington, R. C., & Wilkinson, A. J. (1997). Tension in haemoglobin revealed by Fe-His(F8) bond rupture in the fully liganded T-state. Journal of Molecular Biology, 271(2), pp. 161-7.
Paoli M, et al. Tension in Haemoglobin Revealed By Fe-His(F8) Bond Rupture in the Fully Liganded T-state. J Mol Biol. 1997 Aug 15;271(2):161-7. PubMed PMID: 9268649.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Tension in haemoglobin revealed by Fe-His(F8) bond rupture in the fully liganded T-state. AU - Paoli,M, AU - Dodson,G, AU - Liddington,R C, AU - Wilkinson,A J, PY - 1997/8/15/pubmed PY - 1997/8/15/medline PY - 1997/8/15/entrez SP - 161 EP - 7 JF - Journal of molecular biology JO - J. Mol. Biol. VL - 271 IS - 2 N2 - In 1972, Perutz proposed that the low affinity of T-state haemoglobin is caused by tension in the bond between the iron and the proximal histidine, restraining the Fe from moving into the porphyrin plane on binding oxygen. This proposal has often been disputed. If such tension does exist, it will be manifest in the liganded T-state. Here we describe the structure of the fully liganded T-state cyanide complex of haemoglobin, in which the Fe-proximal histidine bond in the alpha-subunits, but not in the beta-subunits, is ruptured. This rupture uncouples the structural changes at the alpha-haem from those in the globin and the beta-haem, and demonstrates unequivocally the existence of tension and its transmission through this bond. SN - 0022-2836 UR - https://www.unboundmedicine.com/medline/citation/9268649/Tension_in_haemoglobin_revealed_by_Fe-His(F8)_bond_rupture_in_the_fully_liganded_T-state L2 - https://linkinghub.elsevier.com/retrieve/pii/S0022-2836(97)91180-3 DB - PRIME DP - Unbound Medicine ER -