Preliminary time-of-flight neutron diffraction study of human deoxyhemoglobin
Journal Article
·
· Acta Crystallographica. Section F
- Bioscience Division, MS M888, Los Alamos National Laboratory, Los Alamos, NM 87545 (United States)
- Kyoto University, Research Reactor Institute, Kumatori, Osaka 590-0494 (Japan)
- Jichi Medical University, Department of Physiology, Shimotsuke, Tochigi 329-0498 (Japan)
- Yokohama City University, Graduate School of Integrated Science, Tsurumi, Yokohama 230-0045 (Japan)
In order to investigate the role of the protonation states of protein residues in O{sub 2} binding, large crystals of deoxy HbA (∼20 mm{sup 3}) were grown in D{sub 2}O under anaerobic conditions for neutron diffraction studies. Human hemoglobin (HbA) is an intricate system that has evolved to efficiently transport oxygen molecules (O{sub 2}) from lung to tissue. Its quaternary structure can fluctuate between two conformations, T (tense or deoxy) and R (relaxed or oxy), which have low and high affinity for O{sub 2}, respectively. The binding of O{sub 2} to the heme sites of HbA is regulated by protons and by inorganic anions. In order to investigate the role of the protonation states of protein residues in O{sub 2} binding, large crystals of deoxy HbA (∼20 mm{sup 3}) were grown in D{sub 2}O under anaerobic conditions for neutron diffraction studies. A time-of-flight neutron data set was collected to 1.8 Å resolution on the Protein Crystallography Station (PCS) at the spallation source run by Los Alamos Neutron Science Center (LANSCE). The HbA tetramer (64.6 kDa; 574 residues excluding the four heme groups) occupies the largest asymmetric unit (space group P2{sub 1}) from which a high-resolution neutron data set has been collected to date.
- OSTI ID:
- 22360513
- Journal Information:
- Acta Crystallographica. Section F, Journal Name: Acta Crystallographica. Section F Journal Issue: Pt 4 Vol. 64; ISSN ACSFCL; ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
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