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 7
The distal histidines, α₁His58(E7) and β₁His63(E7): alternate protonation states. In the α₁β₁ dimer of T-state HuDeoxyHb both distal histidines are doubly protonated (a) (α₁ is shown, but β₁ is similar), while in the α₂β₂ dimer of T-state HuDeoxyHb (b) (α₂ is shown, but β₂ is similar) both distal histidines are singly protonated. With the presence of ligand in R-state EqCNmetHb (c) (α is shown, but β is similar), the coordinated water molecule is displaced, the singly protonated distal His is hydrogen-bonded to the ligand and Lys(E10) becomes coupled to the heme proprionate group and to His(E7) through a bound water.

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

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

doi:10.1107/S2059798316009049

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