448 IRON-CONTAINING PROTEINS AND ENZYMES
TABLE 7.10 Selected Bond Distances and Angles for Oxidized CcO Enzymes and
Fe
O
Cu
III
II
−−()
2 -- 2
or Fe
III
- (OH
- ) – Cu
II Model
Complexes CcO Crystal Structure or Model Compound
Bridging
Ligand
Fe · · · Cu
Distance (
Å )
Fe · · · X
a
Distance ( Å )
Cu · · · Y(X)
Distance (
Å )
Fe – X – Cu Angle ( ° )
PDB: 2OCC (bovine heart)
O
2 − 2
(possible)
4.85
2.28
2.02
119.6 (O2), 157.6 (O3)
R. sphaeroides
b (PDB: 1M56, 1M57)
OH
− or H
O 2
4.8
3.6
2.0
T. thermophilus
c (PDB: 1EHK)
O
2 −
, OH
− , or H
O 2
4.4
2.3
2.3
[(F
TPP)Fe 8
III
- (O
2 −
) – Cu
II (TMPA)]
+^
O
2 −
3.60
1.74
1.86
178
[(F
TPP)Fe 8
III
- (OH
- ) – Cu
II (TMPA)]
+d
OH
−^
3.66
1.87
1.89
157
[(
6 L)Fe
III
- O – Cu
II ]
+e
O
2 −
3.59
1.75
1.85
171
[(
5 L)Fe
III
- O – Cu
II ]
+d,e
O
2 −
3.40
1.77
1.84
141
a X equals the possible bridging ligands
O
2 − 2
, O
2 − , OH
− , or H
O. 2
b 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.