Fig. 4: Protonation states of Tyr166 and His30 in Tyr34Phe MnSOD between adjacent subunits across the dimeric protein-protein interface. | Nature Communications

Fig. 4: Protonation states of Tyr166 and His30 in Tyr34Phe MnSOD between adjacent subunits across the dimeric protein-protein interface.

From: The role of Tyr34 in proton coupled electron transfer and product inhibition of manganese superoxide dismutase

Fig. 4

a, b Neutron structures of D2O2-soaked Tyr34Phe MnSOD (2.3 Å resolution). c, d Neutron structures of Tyr34Phe Mn2+SOD (2.5 Å resolution). e, f Neutron structures of Tyr34Phe Mn3+SOD (2.3 resolution). Blue, green, and orange omit |Fo| - |Fc| difference neutron scattering length density of protons displayed at 2.0 σ, 2.5σ, and 3.0σ, respectively. Light blue 2|Fo | - |Fc| density is displayed at 1.0σ. Distances are in Å. Dashed lines indicate hydrogen bonds ≥ 1.8 Å and hashed lines indicate SSHBs that are hydrogen bonds < 1.8 Å. Chains are colored according to the inset in Fig. 4a.

Back to article page