Oxygen binding to α-subunits in high-salt crystals of T-state hemoglobin

Gregory B. Vásquez, Xinhua Ji, Igor Pechik, Clara Fronticelli, Gary L. Gilliland

Research output: Contribution to journalArticlepeer-review

Abstract

The crystal structures of a partially-oxygenated, human, T-state hemoglobin variant, βC112G, and a deoxy structure of a related hemoglobin construct, β(C93A+C112G), have been determined at 2.0 Å and 1.8 Å resolution, respectively. Oxygen molecules fully occupy the α1-heme and partially occupy the α2-heme binding sites of the βC112G mutant hemoglobin. Comparisons of these structures with deoxy-, oxy-, and carboxyhemoglobin provide insight into hemoglobin's allosteric transition.

Original languageEnglish (US)
Pages (from-to)59-66
Number of pages8
JournalProtein and Peptide Letters
Volume6
Issue number2
StatePublished - 1999
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry

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