ArticleScientific reports2017
Tertiary and quaternary structural basis of oxygen affinity in human hemoglobin as revealed by multiscale simulations.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Immersive virtual reality for teaching hemoglobin structure in preclinical medical biochemistry education: a mixed-methods study of student self-reported perceptions.BMC medical education · 2026Article
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- A structure and function-based complete mutational map of human hemoglobin using AI.Frontiers in chemistry · 2026Article
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- Evaluating sheep hemoglobins with MD simulations as an animal model for sickle cell disease.Scientific reports · 2024Article
- How purposeless physics underlies purposeful life.Nature · 2023Article
- A retrospective on statistical mechanical models for hemoglobin allostery.The Journal of chemical physics · 2022Article
- Impact of hemoglobin biophysical studies on molecular pathogenesis and drug therapy for sickle cell disease.Molecular aspects of medicine · 2022Review
- Analysis of Fluctuation in the Heme-Binding Pocket and Heme Distortion in Hemoglobin and Myoglobin.Life (Basel, Switzerland) · 2022Article
- Dynamics of camel and human hemoglobin revealed by molecular simulations.Scientific reports · 2022Article
- Carbon Dioxide and the Carbamate Post-Translational Modification.Frontiers in molecular biosciences · 2022Review
- Sample Processing and Stability for Urine Biomarker Studies.The journal of applied laboratory medicine · 2021Article
- Advanced Bioluminescence System for In Vivo Imaging with Brighter and Red-Shifted Light Emission.International journal of molecular sciences · 2020Review
- Structure and function of crocodilian hemoglobins and allosteric regulation by chloride, ATP, and COAmerican journal of physiology. Regulatory, integrative and comparative physiology · 2020Article
- The importance of the quaternary structure to represent conformational ensembles of the major Mycobacterium tuberculosis drug target.Scientific reports · 2019Article
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5 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Human hemoglobin (Hb) is a benchmark protein of structural biology that shaped our view of allosterism over 60 years ago, with the introduction of the MWC model based on Perutz structures of the oxy(R) and deoxy(T) states and the more recent Tertiary Two-State model that proposed the existence of individual subunit states -"r" and "t"-, whose structure is yet unknown. Cooperative oxygen binding is essential for Hb function, and despite decades of research there are still open questions related to how tertiary and quaternary changes regulate oxygen affinity. In the present work, we have determined the free energy profiles of oxygen migration and for HisE7 gate opening, with QM/MM calculations of the oxygen binding energy in order to address the influence of tertiary differences in the control of oxygen affinity. Our results show that in the α subunit the low to high affinity transition is achieved by a proximal effect that mostly affects oxygen dissociation and is the driving force of the allosteric transition, while in the β subunit the affinity change results from a complex interplay of proximal and distal effects, including an increase in the HE7 gate opening, that as shown by free energy profiles promotes oxygen uptake.
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