Table 1.

C1 model systems and their simulation lengths

Model systemCuAHeme aBNCHis413Asp51Glu242Tyr244Lys319Asp364No. of replica and simulation lengths, ns
C1-IOXOXOX*D (0)P (0)P (0)D (−1)D (0)P (0)1 × 300
3 × 40
C1-IIOXOXOX*D (0)P (0)D (−1)D (−1)D (0)P (0)200
C1-IIIOXOXOX*D (0)P (0)P (0)D (−1)P (+1)P (0)200
C1-IVOXOXOXD (0)P (0)P (0)P (0)D (0)P (0)200
C1-VOXOXOX§D (0)P (0)P (0)D (−1)D (0)P (0)200
C1-VIOXOXOX*P (+1)P (0)P (0)D (−1)D (0)P (0)150
  • Protonation state changes of key amino acid residues (D, deprotonated, P, protonated; net charge in parentheses) compared with the original C1-I simulation are highlighted in bold. The protonation pattern within the BNC in C1-IV and C1-V was varied from that in C1-I as defined in the footnotes. OX, oxidized.

  • * BNC structure of Fe[III]-OH....H2O-Cu[II] TyrO.

  • With hydrated H-channel snapshots taken from C1-VI.

  • BNC structure of Fe[III]-OH....H2O-Cu[II] TyrOH.

  • § BNC structure of Fe[III]-H2O....H2O-Cu[II] TyrO.