Table 1.
UV and Visible Optical Absorbance Spectra of Different Myoglobin Forms, Ferriprotoporphyrin IX (Hemin), and a Hemin Degradation Product
| Form | Soret peak (nm) | Visible range peak(s) (nm) | Visible range peak(s) (nm) | References |
|---|---|---|---|---|
| O2(II)Mb | 418 | 543 | 581 | (5) |
| deoxy(II)Mb | 435 | 560 | (5) | |
| met(III)Mb | 408 | 502 | 630 | (5) |
| Mb(IV)=O | 420 | 549 | 582 (shoulder) | (33, 55) |
| Crosslinked Mb (pH 7.0) | 405–408 | 589 | (50, 59) | |
| Crosslinked Mb (pH 1.9) | 398 | 482, 546 | 580, 720 | (59) |
| Hemichrome | 415 | 535 | 565 (shoulder) | (17) |
| Hemochromea | 529 | 558 | (53) | |
| CO(II)Mb | 424 | 540 | 579 | (5) |
| NO(II)Mb | 421 | 543 | 575 | (5) |
| CN(III)Mb | 423 | 540 | 560 (shoulder) | (5) |
| Sulf(II)Mb | 420 | 617 | (46) | |
| Sulf(III)Mb | 404 | 595 | 715 | (46) |
| Heminb | 384 | 508, 538 | 639 | (12) |
| Biliverdinc | 350 | 674 | (82) |
a
Reported for hemoglobin (Hb) β chain.
b
When present in 90% acetone, 8% water, and 2% HCl (12 N).
c
Biliverdin results from enzymatic reaction of heme oxygenase with hemin.
Mb, myoglobin.