Table 2.
Comparison of Published Copper Self-Exchange Rate Constants (k11) and Reorganization Energies (λ) for Species Depicted in Figure 4
| λ (eV) | k11 (M−1 s−1) | conditions | reference | ||
|---|---|---|---|---|---|
| type I proteins | azurin (CuII,I) | 0.82 | 7.94 × 105 to 1.26 × 106 | H2O, 25 °C | 30–32 |
| plastocyanin (CuII,I) | 0.72 | 3.16 × 105 to 6.31 × 105 | H2O, 25 °C | 33, 34 | |
| nitrite reductase (CuII,I) | 0.77 | – | H2O, 25 °C | 41 | |
| “classical” copper(II,I) complexes | [CuII,I(phen)2]2+/+ | 2.4 | 50 | H2O, 22 °C | 26–28 |
| 0.2 | CH3CN, 25 °C | ||||
| [CuII,I(bipy)2]2+/+ | 1.88 | 4.4 × 103 | H2O, 25 °C | 27 | |
| [CuII,I(bib)2] | 2.8c | 0.16 | CH3CN, 25 °C | 53 | |
| constrained copper(II,I) complexes | [CuII,I(dmp)2]2+/+ | 2.28c | 23 | CH3CN, 25 °C | 54 |
| [CuII,I(SC6F5)(iprtpz)]0/+ | 1.58c | 1.76 × 104 | acetone-d6, −20 °C | 55 | |
| 3.14 × 105 | acetone-d6, 25 °C | ||||
| [CuII,I(H2TpyNMes)Cl]+/0 | 1.33c | 2.4 × 105 | THF, 25 °C | 46 | |
| [CuII,I(TMGqu)2]2+/+ | 0.77 | 1.2 × 104 | CH3CH2CN, 20 °C | 36, 37 | |
| 4.2 × 10−3 | CH2Cl2, −90 °C | ||||
| [CuII,I(DMEGqu)2]2+/+ | 0.89 | 5.4 × 102 | CH3CH2CN, 20 °C | 36 | |
| [CuII(UN-O−)(O2•−/O22−)]2+/+ | 0.81a | – | CH2Cl2, −80 °C | 42 | |
| copper(III,II) complexes | [LCuIII,II(OH)]0/− | 0.95 | 3 × 104 | CH2Cl2, −88 °C | this work |
| 9 × 106 | CH2Cl2, 25 °C | this work | |||
| [CuIII,IIHLn]2+/+ | b | 5 × 105 | H2O, 25 °C | 13 | |
| [CuIII,II(H−2Aib3)]0/− | 1.48c | 5.5 × 104 | H2O, 25 °C | 12 |
a
The reorganization energy of the [CuII(ON-O−)(O2•−/O22−)]2+/+ self-exchange was determined by calculating λo for the complex in CH2Cl2 at −80 °C (using eq 4 and the information in the Supporting Information of ref 42) and adding this value to the computed value of λin.
b
The reported k11 for this complex may have been derived incorrectly using parameters from PCET steps.13 Therefore, no λ was estimated for this complex.
c
Calculated from eq 1 using the measured k11.