448 IRON-CONTAINING PROTEINS AND ENZYMES
TABLE 7.10 Selected Bond Distances and Angles for Oxidized CcO Enzymes andFeOCuIIIII−−()2 -- 2or FeIII- (OH
- ) – Cu
II ModelComplexes CcO Crystal Structure or Model CompoundBridgingLigandFe · · · Cu
Distance (Å )Fe · · · XaDistance ( Å )Cu · · · Y(X)
Distance (Å )Fe – X – Cu Angle ( ° )PDB: 2OCC (bovine heart)O2 − 2(possible)4.852.282.02119.6 (O2), 157.6 (O3)R. sphaeroidesb (PDB: 1M56, 1M57)OH− or HO 24.83.62.0T. thermophilusc (PDB: 1EHK)O2 −
, OH− , or HO 24.42.32.3[(FTPP)Fe 8III- (O
2 −
) – CuII (TMPA)]+^O2 −3.601.741.86178[(FTPP)Fe 8III- (OH
- ) – Cu
II (TMPA)]+dOH−^3.661.871.89157[(6 L)FeIII- O – Cu
II ]+eO2 −3.591.751.85171[(5 L)FeIII- O – Cu
II ]+d,eO2 −3.401.771.84141a X equals the possible bridging ligandsO
2 − 2
, O2 − , OH− , or HO. 2b Reference 144. c Reference 157. d Bond distances and angles determined by X - ray absorption spectroscopy (XAS) methods. See reference 138 and Figures 7.4
4 and 7.47.e References 138 and 159.