Visualizing the Bohr effect in hemoglobin: neutron structure of equine cyanomethemoglobin in the R state and comparison with human deoxyhemoglobin in the T state

Dajnowicz, S.; Seaver, S.; Hanson, B.L.; Fisher, S.Z.; Langan, P.; Kovalevsky, A.Y.; Mueser, T.C.

doi:10.1107/S2059798316009049

Acta Crystallographica Section D
Acta Crystallographica
Section D STRUCTURAL BIOLOGY

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Figure 6
βHis117(G19) counters the alkaline Bohr effect. Solvent-exposed and located near the end of the G helix, βHis117(G19) appears to be singly protonated with dual conformation in T-state HuDeoxyHb β₁ (a), singly protonated in the T-state HuDeoxyHb β₂ chain (b) and doubly protonated in R-state EqCNmetHb β (c). βHis116(G18) is doubly protonated in the T state (a, b) but is not conserved (c).

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

Volume 72| Part 7| July 2016| Pages 892-903

doi:10.1107/S2059798316009049

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