Table 3. Overview of Experimentally Determined Thermodynamic Constants Describing the Affinity of Metalloproteins for Select Trivalent Actinides (Ac3+, Am3+, Cm3+, and Cf3+), as well as for Tetravalent Actinides (Th4+ and Pu4+) and Uranyl (UO22+)a.
protein | reaction | thermodynamic constant | conditions | ref |
---|---|---|---|---|
transferrin (Tf) | Pu4+ + Tf = PuCTf | log K11 = 24.8 | pH 6.0, synergistic ion = NTA. I = 0.1 M NaCl, MES buffer | (96) |
Pu4+ + Tf = PuCTf | log K11 = 26.44 | pH 7.0, synergistic ion = NTA. I = 0.1 M | (99) | |
Fe3+ + Tf = Fe2Tf | log K11 = 21.4 | pH 7.4, Ambient pCO2. | (37) | |
Fe3+ + FeTf = Fe2Tf | log K21 = 20.3 | |||
2 Fe3+ + Tf = Fe2Tf | log β21 = 41.7 | |||
Cm3+ + Tf = CmCTf | log K11 = 8.8 (C-lobe) | pH 8.6, 50 mM Tris, 150 mM NaCl, 5 mM NaHCO3 | (38) | |
Cm3+ + CmCTf = Cm2Tf | log K21 = 7.0 (N-lobe) | |||
2 Cm3+ + Tf = Cm2Tf | log β21 = 15.8 | |||
2 Ac3+ + Tf = Ac2Tf | log β21 = 10.9 | Estimate based on literature data and a linear free-energy relationship. | (119) | |
fetuin (Fet) | Pu4+ + Fet = PuFet | log K11 = 26.2 | pH 7.0. I = 0.1 M | (99) |
UO22+ + Fet = UO2Fet | log K11 = 7.5 (Kd = 30 nM) | pH 7.4, 140 mM NaCl, pCO2 | (97) | |
human serum albumin (HSA) | Th4+ + HSA = ThHSA | log K11 = 4.12 | pH ∼7.4, 5 mM HEPES, 150 mM NaCl | (100) |
UO22+ + HSA = UO2HSA | log K11 = 4.27 | pH ∼7.4, 5 mM HEPES, 150 mM NaCl | (100) | |
lanmodulin (LanM) | wild-type lanmodulin: 3 Ac3+ + LanM = Ac3LanM | log β31 = 36.2 | pH 7.0, 90 mM NaCl, 10 mM HEPES | (119) |
wild-type lanmodulin: 3 Am3+ + LanM = Am3LanM | log β31 = 35.6 | pH 5.0, 75 mM NaCl, 25 mM acetate | (50) | |
3 Cm3+ + LanM = Cm3LanM | log β31 = 35.8 | pH 5.0, 75 mM NaCl, 25 mM acetate | (50) | |
lanmodulin variants: | log β31 = 34.4 | pH 5.0, 75 mM NaCl, 25 mM acetate | (120) | |
3 Am3+ + 3D9N = Am33D9N | ||||
3 Am3+ + 3D9A = Am33D9A | log β31 = 33.1 | |||
3 Am3+ + 3D9M = Am33D9M | log β31 = 32.3 | |||
3 Am3+ + 3D9SeMet = Am33D9SeMet | log β31 = 32.4 | |||
3 Am3+ + 3D9H = Am33D9H | log β31 = 32.6 | |||
alpha amylase (Amy) | Cm3+ + Amy = CmAmy | log K11 = 4.76 | pH 5.5, I = 0.1 M | (105) |
Cm3+ + 3 Amy = Cm(Amy)3 | log β13 = 12.14 | |||
UO22+ + Amy = UO2Amy | log K11 = 5.67 | I = 0.1 M (NaCl) | (107) | |
UO22+ + 2 Amy = UO2(Amy)2 | log β12 = 10.39 | |||
UO22+ + Amy + HO– = UO2(HO)Amy | log K11–1 = 0.64 | |||
UO22+ + Amy +2 HO– = UO2(HO)2Amy | log β11–2 = −6.28 | |||
osteopontin (OPN) | x UO22+ + OPN = (UO2)xOPN | (Kd = 26 nM)* | *Number of binding sites undetermined. | (103) |
siderocalin (Scn) | [PuIVEnterobactin]2– + Scn = [PuIVEnterobactin]/Scn | log K11 = 10.0 (Kd = 0.09 nM) | pH 7.4, TBS buffer, 10 μg/mL ubiquitin, 5% DMSO. Actinide precomplexed to enterobactin. | (102) |
[FeIIIEnterobactin]2– + Scn = [FeIiiEnterobactin]/Scn | log K11 = 9.4 (Kd = 0.41 nM) | pH 7.4, TRIS buffer, 32 μg/mL ubiquitin. | (121) | |
[AmEnterobactin]3– + Scn = [AmEnterobactin]/Scn | log K11 = 9.6 (Kd = 0.24 nM) | pH 7.4, TBS buffer, 10 μg/mL ubiquitin, 5% DMSO. Actinide precomplexed to enterobactin. | (102) | |
[CmEnterobactin]3– + Scn = [CmEnterobactin]/Scn | log K11 = 9.7 (Kd = 0.20 nM) | pH 7.4, TBS buffer, 10 μg/mL ubiquitin, 5% DMSO. Actinide precomplexed to enterobactin. | (102) | |
[Am343-LI(1,2-HOPO)]− + Scn = [Am343-LI(1,2-HOPO)]/Scn | log K11 = 7.5 (Kd = 29 nM) | pH 7.4, TBS buffer, 10 μg/mL ubiquitin, 5% DMSO. Actinide precomplexed to ligand. | (102) | |
[Cm343-LI(1,2-HOPO)]− + Scn = [Cm343-LI(1,2-HOPO)]/Scn | log K11 = 7.5 (Kd = 32 nM) | pH 7.4, TBS buffer, 10 μg/mL ubiquitin, 5% DMSO. Actinide precomplexed to ligand. | (102) | |
[Cf343-LI(1,2-HOPO)]− + Scn = [Cf343-LI(1,2-HOPO)]/Scn | log K11 = 7.3 (Kd = 50 nM) | pH 7.4, TBS buffer, 10 μg/mL ubiquitin, 5% DMSO. Actinide precomplexed to ligand. | (23) | |
synthetic peptides (LBT) | Am3+ + LBT = AmLBT | log K11 = 7.35 (Kd = 45 nM) | pH 7, 10 mM HEPES/100 mM NaCl buffer, | (122) |
Corresponding constants for ferric iron (Fe3+) are also given for comparison. Although not proteins, synthetic lanthanide peptides (LBTs) are also shown for the sake of comparison. The Kd values reported in this table correspond to protein binding constants, not solubility products (also abbreviated Kd in the literature).