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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.