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Table 1 Comparison of model FeL complex formation and dissociation rate constants, conditional stability constants, and Fe' and Fe3+residence times in treated with Chelex, photo-irradiated seawater as determined using the kinetic method. Errors represent average mean ± s (standard deviation) from two separate replicates.[1] Data taken from ref. 12

From: Metal–organic complexation in the marine environment

Model ligand kf × 105/M-1s-1 kd × 10-6/s-1 log KFe'L kinetic log K Fe 3+ L kinetic Fe' residence time/yr Fe3+ residence time/yr log Ktherm
Protoporphyrin IXa 6.2 ± 0.8 0.7 ± 0.7 11.9 ± 0.5 21.9 ± 0.5 0.031 645 --
Protoporphyrin IX Dimethyl estera 15.3 ± 0.2 0.2 ± 0.9 13.0 ± 0.2 23.0 ± 0.2 0.116 5866 --
Phaeophytina 12.2 ± 0.1 12.3 ± 16.8 11.0 ± 1.2 21.0 ± 1.2 0.002 72 --
Apoferritinb 0.93 ± 0.3 0.08 ± 0.04 12.1 ± 0.1 22.1 ± 0.1 0.275 820 --
Phytic acidc 12.8 ± 0.1 0.51 ± 0.28 12.4 ± 0.2 22.4 ± 0.2 0.043 1820 --
Alterobactin Ad 3.8 ± 0.8 0.17 ± 0.04 12.3 ± 0.4 22.3 ± 0.4 0.129 1620 49–5318
Alterobactin Be 8.0 ± 0.6 0.25 ± 0.02 12.5 ± 0.3 22.5 ± 0.3 0.088 2330 43.648
Enterobactin1f 10 15.8 10.8 20.8 0.013 46.0 49.020
Ferrichromeg 4.6 ± 2.9 0.05 ± 0.04 12.9 ± 0.1 22.9 ± 0.1 0.439 6700 29.0731
Desferrioxamineg 19.6 ± 10.1 1.5 ± 1.8 12.1 ± 0.6 22.1 ± 0.6 0.015 952 30.6031
  1. Fe complexing moieties for the model ligands: aPorphyrin. bProtein. cPhosphate. dβ-Hydroxyaspartate/catecholate. eBis-catecholate. fTris-cate-cholate. gtris-Hydroxamate.