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. Author manuscript; available in PMC: 2010 Apr 5.
Published in final edited form as: Biochemistry. 2009 Jul 28;48(29):7056–7071. doi: 10.1021/bi900697c

Table 1.

Comparison of electronic absorption and MCD peak positions for low-spin, 6-coordinate Fe(III) heme proteins. The experimental values for Rev-erbβ (LBD) and E75(LBD) are shaded.

Electronic Absorption

Protein Ligands δ Soret β α LMCT Ref.
Rev-erbβ (LBD) X/Cys 359 420 541 563 664, 757 a
E75(LBD) X/Cys 360 423 542 569 650, 750 a
E75(261) N-,O-,S-?/Cysn 359 424 542 575 NRb (23)
RrCooA Pro/Cys 362 424 540 574 649,750 (46)
P450CAM+ImH ImH/Cys 358 425 542 574 638,753 (73)
hCBS His/Cys 365 428 550 NR 650,700 (35)
M80C cyt c His/Cys 355 416 540 570 635,734 (73)

MCD Peak Crossover Trough Peak Crossover Trough Ref.

Rev-erbβ(LBD) X/Cys 404 412 427 562 571 579 a
E75(LBD) X/Cys 414 421 429 NRb NRb NRb a
RrCooA Pro/Cys 413c 420 427c 562c 571 580b (47)
P450CAM+ImH ImH/Cys 417 426 435 563 569 585 (74)
hCBSc His/Cys 419 425 433 545 555 567 (35)
M80C cyt c His/Cys 415c 424c 432 b MSd 560c MSd (74)
a

This work.

b

Not reported.

c

Negligible intensity.

d

Peak and/or crossover positions were not reported in the original paper and are presented from inspection of the data.

e

Multiple max/crossover/min signals are present; only that of the central crossover position is indicated.