. 2013 Apr 18;110(19):7690–7695. doi: 10.1073/pnas.1300817110

Table 1.

H-bond distances for TyrD in QM/MM optimized geometries in the PSII protein environment (measured in angstroms)

Redox/protonation state	O_TyrD−N_ε,His	O_TyrD–H	H–N_ε,His	O_TyrD−O_H2O	N_δ,His−N_Arg
Original (1.9-Å structure)	2.74	—	—	Distal, 4.30; proximal, 2.73	2.81
TyrD-OH (Fig. 2, Left)
	2.78	1.77	1.02	2.78	2.89
TyrD-O^• (Fig. 2, Right)
	2.78	1.77	1.02	4.23	2.90
	2.71	0.99	1.72	4.13	2.92

Note that the Inline graphic state was energetically very unstable and that only the state was possible. Arg, D2-Arg294; Glu, CP47-Glu364; His, D2-His189; —, not applicable.