ArticleActa crystallographica. Section D, Biological crystallography2010
Protonation states of histidine and other key residues in deoxy normal human adult hemoglobin by neutron protein crystallography.
Article in Acta crystallographica. Section D, Biological crystallography, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Advantages of Increasing Histidine to Lysine Ratios on Growth Performance, Blood Parameters and Histidine-Containing Dipeptides for Weaning Piglets.Animals : an open access journal from MDPI · 2026Article
- A pH-sensitive motif in an outer membrane protein activates bacterial membrane vesicle production.Nature communications · 2024Article
- The effects of standardized ileal digestible His to Lys ratio on growth performance, intestinal health, and mobilization of histidine-containing proteins in pigs at 7 to 11 kg body weight.Journal of animal science · 2023Article
- AltitudeOmics: Red Blood Cell Metabolic Adaptation to High Altitude Hypoxia.Journal of proteome research · 2016Article
Corrections and comments
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Authors and funding
9 authors.
Funding
Abstract
The protonation states of the histidine residues key to the function of deoxy (T-state) human hemoglobin have been investigated using neutron protein crystallography. These residues can reversibly bind protons, thereby regulating the oxygen affinity of hemoglobin. By examining the OMIT F(o)-F(c) and 2F(o)-F(c) neutron scattering maps, the protonation states of 35 of the 38 His residues were directly determined. The remaining three residues were found to be disordered. Surprisingly, seven pairs of His residues from equivalent α or β chains, αHis20, αHis50, αHis58, αHis89, βHis63, βHis143 and βHis146, have different protonation states. The protonation of distal His residues in the α(1)β(1) heterodimer and the protonation of αHis103 in both subunits demonstrates that these residues may participate in buffering hydrogen ions and may influence the oxygen binding. The observed protonation states of His residues are compared with their ΔpK(a) between the deoxy and oxy states. Examination of inter-subunit interfaces provided evidence for interactions that are essential for the stability of the deoxy tertiary structure.
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