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 4
Alternate protonation states of αHis20(B1) and αHis112(G19). Located on the surface near the α₁:β₁ interface, αHis20(B1) is doubly protonated in T-state HuDeoxyHb α₁ (a), singly protonated in T-state HuDeoxyHb α₂ (b) and doubly protonated in R-state EqCNmetHb α (c), while αHis112(G19) is doubly protonated in T-state HuDeoxyHb α₁ and α₂ (a, b) and singly protonated in R-state EqCNmetHb α (c).

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

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

doi:10.1107/S2059798316009049

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