Table 3.
Redesigned Proteins with Copper Electron Transfer Centers
| protein | LMCT λmax (ε/M−1 cm−1)/nm | Em°/mV vs NHE | bond length/Å | EPR g (A/G) | other notes | ref |
|---|---|---|---|---|---|---|
| Cys112Sec-Az | 677(~4000) | 316 ± 2 | Se–Cu(II) 2.30(2) | gx = 2.047 | 388,389 | |
| 2N(imi)–Cu(II) 1.97(2) | gy = 2.109 | |||||
| Se–Cu(I) 2.33(2) | gz = 2.234(104) | |||||
| 2N(imi)–Cu(I) 2.00(2) | ||||||
| Met121Nle-Az | 630(~5000) | 449 ± 3 | S(cys)–Cu(II) 2.19(1) | gx = 2.0402(13.4) | 390,391 | |
| 2N(imi)–Cu(II) 1.95(1) | gy = 2.0584(19.6) | |||||
| S(Cys)–Cu(I) 2.24(1) | gz = 2.2680(58.8) | |||||
| 2N(imi)–Cu(I) 2.02(1) | ||||||
| Met121Leu-Az | 631(~5000) | 450 | S(Cys)–Cu(I) 2.23(1) | gx = 2.0395(13.2) | 390 | |
| 2N(imi)–Cu(I) 2.01(1) | gy = 2.0578(19.2) | |||||
| gz = 2.2706(57.0) | ||||||
| Met121SeM-Az | 629(~5000) | 348 ± 4 | S(Cys)–Cu(II) 2.18(1) | gx = 2.0383(13.2) | 390,391 | |
| 2N(imi)–Cu(II) 1.95(1) | gy = 2.0565(12.1) | |||||
| gz = 2.2585(60.6) | ||||||
| S(Cys)–Cu(I) 2.26(1) | ||||||
| Met121DFM-Az | 628 | 329 ± 5 | 2N(imi)–Cu(I) 2.02(1) | gx = 2.0274(1.9) | 391 | |
| gy = 2.0583(2.0) | ||||||
| gz = 2.2530(56.8) | ||||||
| Met121TFM-Az | 629 | 379 ± 4 | gx = 2.0295(1.9) | 391 | ||
| gy = 2.0583(1.8) | ||||||
| gz = 2.2530(56.8) | ||||||
| Met121OxM-Az | 624 | 222 ± 5 | gx = 2.0305(0.8) | 391 | ||
| gy = 2.0576(2.5) | ||||||
| gz = 2.2629(55.7) | ||||||
| Met121Cys-Az | 451, 627, pH 4.0; 430, 591, pH 9.0 | 95 ± 3, pH 7.0 | S(Cys1)–Cu(II) 2.17(2) | gz = 2.26(58) pH 4.0; gz = 2.25(93) pH 9.0* | *major species | 392 |
| S(Cys2)–Cu(II) 2.74(2) | ||||||
| 2N–Cu(II) 1.95(2) (pH 7.0) | ||||||
| Met121Hcy-Az | 410, 590 | 113 ± 6, pH 7.0 | S(Cys)–Cu(II) 2.22(2), S(Hcy)–Cu (II) 2.79(2), 2N–Cu(II) 1.97(2) | gz = 2.25(193) | 392 | |
| N47S/F114N/M121L-Az | 630(~2080) | 706 ± 3, pH 4.0; 668 ± 1, pH 6.0; 640 ± 1, pH 7.0 | gx = 2.024(11) | (1) EPR spectrum collected at pH 6.0; (2) kET = 78 ± 12 s−1 at 298 K | 3,393 | |
| gy = 2.062(11) | ||||||
| gz = 2.287(44) | ||||||
| F114P/M121Q-Az | 600(~4030) | 90 ± 8, pH 7.0; −2 ± 13, pH 9.0 | S(Cys)–Cu(II) 1.95 | gx = 2.031(6) | (1) EPR spectrum collected at pH 7.0; (2) kET = 81 ± 11 s−1 at 298 K | 3,393 |
| N(His)–Cu(II) 1.95 | gy = 2.047(6) | |||||
| N(Gln)–Cu(II) 2.15 | gz = 2.258(46) | |||||
| CuA-CyoA | 765(900), 536(1600), 358(2000) | 260 ± 10 | gz = 2.20 | 394 | ||
| CuA-Az | 350(380), 485(155), 530(1380), 765(770) | 270, pH 5.0; 239, pH 5.5 | gx = 2.017(28, 15) | kET = 650 ± 60 s−1, pH 5.1, rt | 395–398 | |
| gy = 2.021(21, 14) | ||||||
| gz = 2.169(63, 57) | ||||||
| M123Q-CuA-Az | 350, 485, 530, 800 | 245 ± 6 | gx = 2.013(17, 22) | 397 | ||
| gy = 2.020(21, 19) | ||||||
| gz = 2.170(65, 56) | ||||||
| M123L-CuA-Az | 485, 800 | 255 ± 10 | gx = 2.021(33, 27), 1.982(20); gy = 2.044(32, 20), 2.055(18); gz = 2.168(65, 51), 2.227(30) | valence-delocalized and localized species | 397 | |
| M123D-CuA-Az | 350, 485, 530, 765 | 234 ± 3 | there are two valence-delocalized states | 397 | ||
| gx = 2.004(23, 19), 1.977 | ||||||
| gy = 2.019(24, 21), 2.034 | ||||||
| gz = 2.156(64, 57), 2.267 | ||||||
| M123E-CuA-Az | 350, 485, 530, 855 | 231 ± 3 | gx = 1.989, 1.987; gy = 2.029, 2.038 | there are two valence-delocalized states | 397 | |
| gz = 2.130, 2.263 | ||||||
| N47S-CuA-Az | 483, 530, 753 | 307 ± 7, pH 7.0; 275 ± 14, pH 5.1 | gx = 2.027(24.3) | 399 | ||
| gy = 2.027(14.2) | ||||||
| gz = 2.176(55.8) | ||||||
| E114P-CuA-Az | 473, 535, 784 | 235 ± 3, pH 7.0; 214 ± 8, pH 5.1 | gx = 2.017(29.5) | 399 | ||
| gy = 2.021(10.9) | ||||||
| gz = 2.169(56.6) | ||||||
| CuA-amicyanin (1) | 360, 483, 532, 790 | gx,y = 1.99–2.02 | 400 | |||
| gz = 2.18 (32.4) | ||||||
| CuA-amicyanin (2) | 360(1020), 485(2300), 530(2380), 780(1055) | 273 ± 2 | gx,y = 2.05 | 401 | ||
| gz = 2.20(36) |