Table 1.
Spectral Tuning and Retinal Release Half‐Lives of Great Bowerbird, Chicken, and Bovine Rhodopsins Measured in vitro
| Species | Mutant | 83, 292a | λ max (nm) | t 1/2 (min) |
|---|---|---|---|---|
| P. nuchalis | Wild‐type | N A | 500 | 29.4 |
| P. nuchalis | N83D | D A | 502 (+2) | 18.5 (−10.9) |
| P. nuchalis | A292S | N S | 490 (−10) | 24.4 (−5) |
| G. gallus | Wild‐type | D A | 503 | 17.9 |
| G. gallus | D83N | N A | 501 (−2) | 27.3 (+9.4) |
| B. taurus | Wild‐type | D A | 499 | 15.6 |
| B. taurus | D83N | N A | 495 (−4) | 28.3 (+12.7) |
| B. taurus | A292S | D S | 489 (−10) | 11.4 (−4.2) |
| B. taurus | D83N+A292S | N S | 485 (−14) | 22.2 (+6.6) |
a
83 and 292 refer to the amino acid positions of the rhodopsin protein sequence. The amino acid identities are indicated with standard abbreviations (A, alanine; D, aspartic acid; N, asparagine; S, serine), with colours indicating whether the residue is associated with either a spectral red‐ or blue‐shift.
Numbers in parentheses indicate the functional shift relative to each species' wild‐type condition.