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l max (nm)
(«,mM 1 cm 1 )
Comment References
Ferrous state
Soret
Visible
d
g ba
pH 7.4, e
Synechocystis
(carbonmonoxy)
416
508
(sh)
540
Couture et al.
(2000)
420
(184)
544
(14)
568
(sh)
pH
7.4, b , e
Scott &
Lecomte (2000)
Synechococcus
(carbonmonoxy)
397
(sh)
418
(165)
543
(13)
pH
7.5, b , e
Scott et al.
(2002)
Ferric state
Soret
Visible
d
g
CT
N. commune
(met)
408
(123)
536
(10.3)
570
(sh)
632
(3.28)
pH 7
Thorsteinsson
et al. (1999)
pH 5, d,e
C. eugametos
(met)
406
(130)
529
(6)
624
(2.6)
Couture &
Guertin (1996)
410
(110)
535
(8.5)
pH
7.5, d,e
Couture &
Guertin (1996)
pH 7.4, f
Synechocystis
(met)
362
(sh)
409.5
(100)
544
(11)
578
(sh)
Couture et al.
(2000) & Scott
& Lecomte
(2000)
Synechococcus
(met)
365
(sh)
411
(96)
544
(10)
568
(sh)
pH
7.5, g
Scott et al.
(2002)
N. commune
(cyanomet)
Thorsteinsson
et al. (1996)
- e
C. eugametos
(cyanomet)
416
(97.6)
547
(11)
Couture &
Guertin (1996)
- g
Synechocystis
(cyanomet)
360 416
546
- g
Synechococcus
(cyanomet)
363 416
553
- b
359 415
550
- d
C. eugametos
(azidomet)
413
(105)
543
(9)
580
(sh)
Couture &
Guertin (1996)
a Shoulder.
b Given the method of preparation, the spectrum is for the post-translationally modified protein (covalent
attachment of the haem group to His117, Vu et al., 2002 ).
c
Spectrum presented in the given reference.
d
Data for the H19 construct, with protein product starting at Ser44.
e
The p K a of the transition is 6.3.
f
Extent of post-translational modification unknown.
g No haem post-translational modification.
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