. Author manuscript; available in PMC: 2015 Jan 20.

Published in final edited form as: Chem Rev. 2014 Mar 24;114(7):3495–3578. doi: 10.1021/cr400458x

Table 2.

Redesign and De Novo Designed Heme Proteins

protein	E°/mV vs NHE	UV–vis absorption (Soret band for heme)	other notes	ref
ME1	−128 ± 2	oxidized form: 413 nm	K_{d, app} = (4.7 ± 1.2) × 10⁻⁷ M, 2:1 peptide/hemin stoichiometry	227
		reduced form: 427 nm
Cu_BMb	copper-free: 77, Cu(II)-bound: 80	deoxy-Cu_BMb: 434 nm	oxygen reduction activity	229,260
		oxy-Cu_BMb: 418 nm (not 100% conversion)
Fe_BMb	−46 ± 2	deoxy-Fe_BMb: 433 nm	nitric oxide reductase activity	232
		deoxy-Fe²⁺-Fe_BMb: 434 nm
Fe-porphycene-Mb	−190 ± 15	oxidized form: 387 nm	enhanced O₂ binding affinity	253
		reduced form: 375 nm
		oxy-reduced form: 387 nm
6-propionate Mb	91.7 ± 1.0	Met-rMb: 408 nm	(1) Raman shift of deoxy-form: 220 cm⁻¹; (2) pK_{a(heme-bound water)} = 8.67 ± 0.03	248
		ferrous-rMb: 432 nm
		oxy-rMb: 417 nm
7-propionate Mb	84.6 ± 1.0	Met-rMb: 407 nm	(1) Raman shift of deoxy form: 221 cm⁻¹; (2) pK_{a(heme-bound water)} = 8.73 ± 0.03	248
		ferrous-rMb: 431 nm
		oxy-rMb: 417
heme-6-propionate Cyt P450cam		oxidized form: 391 nm (in the presence of d-camphor)	(1) Raman shift of the ferric form: 351 cm⁻¹; (2) NADH oxidation rate 1150 μM/μM min enzyme⁻¹	251
heme-7-propionate Cyt P450cam		oxidized form: 417 nm (in the presence of d-camphor)	(1) Raman shift of the ferric form: 1503, 1489 cm⁻¹; (2) NADH oxidation rate 27 ± 2 μM/μM min enzyme⁻¹	250
PRIME	−97 ± 3, −168 ± 3	oxidized form: 410 nm	in palmitoyl oleoyl phosphatidylcholine bilayers	261
[Δ7-H₁₀I₁₄I₂₁]₂	−222	oxidized form: 412 nm (131 000 M⁻¹ cm⁻¹)	K_d1^Fe(II) = 42 nM, K_d2^Fe(II) = 15 μM	262
		reduced form: 427 nm (209 000 M⁻¹ cm⁻¹)
[Δ7-Pal₁₀I₁₄I₂₁]₂	58 ± 8	oxidized form: 410 nm (110 000 M⁻¹ cm⁻¹)		263
		reduced form: 420 nm (144 000 M⁻¹ cm⁻¹)
[Δ7-H_1m10I₁₄I₂₁]₂		reduced form: 431 nm (97 000 M⁻¹ cm⁻¹)	vacant coordination site for CO binding	264
Fe(PPIX)-[Δ7-H-H3m]₂	−190 ± 10	oxidized form: 412 nm (123 000 M⁻¹ cm⁻¹)	E° determined at pH 8.0	265
		reduced form: 427 nm (191 00 M⁻¹ cm⁻¹)
Fe(DADPIX)-[Δ7-H-H3m]₂	−30 ± 10	oxidized form: 426 nm (89 000 M⁻¹ cm⁻¹)	E° determined at pH 8.0	265
		reduced form: 450 nm (110 000 M⁻¹ cm⁻¹)
HP7-H7F	−260 ± 6	oxidized form: 414 nm (129 000 M⁻¹ cm⁻¹)	pK_a (His) = 7.3 ± 0.2	266
		reduced form: 428 nm (140 000 M⁻¹ cm⁻¹)
heme-Ru-MOP2	−170 ± 6	oxidized form: 413 nm	electron transfer demonstrated	267
		reduced form: 428 nm
Fe-mimochrome IV	−80 (pH 7.0)	oxidized form: 398 nm		268
miniperoxidase 3		oxidized form: 391 nm	HRP activity	218
immobilized heme-S824C	−153	oxidized form: 413 nm	binds to N-donor ligands	269