Deer mouse hemoglobin exhibits a lowered oxygen affinity owing to mobility of the e helix

Noriko Inoguchi, Jake R. Oshlo, Chandrasekhar Natarajan, Roy E. Weber, Angela Fago, Jay F. Storz, Hideaki Moriyama

Research output: Contribution to journalArticlepeer-review

7 Scopus citations


The deer mouse, Peromyscus maniculatus, exhibits altitude-associated variation in hemoglobin oxygen affinity. To examine the structural basis of this functional variation, the structure of the hemoglobin was solved. Recombinant hemoglobin was expressed in Escherichia coli and was purified by ion-exchange chromatography. Recombinant hemoglobin was crystallized by the hanging-drop vapor-diffusion method using polyethylene glycol as a precipitant. The obtained orthorhombic crystal contained two subunits in the asymmetric unit. The refined structure was interpreted as the aquo-met form. Structural comparisons were performed among hemoglobins from deer mouse, house mouse and human. In contrast to human hemoglobin, deer mouse hemoglobin lacks the hydrogen bond between 1Trp14 in the A helix and 1Thr67 in the E helix owing to the Thr67Ala substitution. In addition, deer mouse hemoglobin has a unique hydrogen bond at the 1β1 interface between residues 1Cys34 and β1Ser128.

Original languageEnglish (US)
Pages (from-to)393-398
Number of pages6
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Issue number4
StatePublished - Apr 2013


  • Peromyscus maniculatus
  • deer mouse
  • hemoglobin
  • oxygen affinity

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics


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