Hemoglobin redux: Combining neutron and X-ray diffraction with mass spectrometry to analyse the quaternary state of oxidized hemoglobins

Timothy C. Mueser, Wendell P. Griffith, Andrey Y. Kovalevsky, Jingshu Guo, Sean Seaver, Paul Langan, B. Leif Hanson

Research output: Contribution to journalArticlepeer-review

1 Scopus citations

Abstract

Improvements in neutron diffraction instrumentation are affording the opportunity to re-examine the structures of vertebrate hemoglobins and to interrogate proton and solvent position changes between the different quaternary states of the protein. For hemoglobins of unknown primary sequence, structural studies of cyanomethemoglobin (CNmetHb) are being used to help to resolve sequence ambiguity in the mass spectra. These studies have also provided additional structural evidence for the involvement of oxidized hemoglobin in the process of erythrocyte senescence. X-ray crystal studies of Tibetan snow leopard CNmetHb have shown that this protein crystallizes in the B state, a structure with a more open dyad, which possibly has relevance to RBC band 3 protein binding and erythrocyte senescence. R-state equine CNmetHb crystal studies elaborate the solvent differences in the switch and hinge region compared with a human deoxyhemoglobin T - state neutron structure. Lastly, comparison of histidine protonation between the T and R state should enumerate the Bohr-effect protons.

Original languageEnglish (US)
Pages (from-to)1249-1256
Number of pages8
JournalActa Crystallographica Section D: Biological Crystallography
Volume66
Issue number11
DOIs
StatePublished - Nov 2010
Externally publishedYes

Fingerprint Dive into the research topics of 'Hemoglobin redux: Combining neutron and X-ray diffraction with mass spectrometry to analyse the quaternary state of oxidized hemoglobins'. Together they form a unique fingerprint.

Cite this