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Comments on Inorganic Chemistry
A Journal of Critical Discussion of the Current Literature
Volume 2, 1983 - Issue 3-4
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Original Articles

On Carbon Monoxide and Dioxygen Binding by Iron(II) Porphyrinato Systems

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Pages 97-126 | Published online: 19 Dec 2006

References

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  • The following relevant numbers for micelle-heme systems have been published. They are derived from separate, independent measurements and thus provide an indication of the accuracy obtainable in the measurement of kinetic parameters in micellar systems. For O2 binding to chelated mesoheme in 2% myristyltrimethylammonium bromide (MTAB) at 20°C values for K o2 of 1.3 × 106 M−1 (Ref. 4 referring to Ref. 33) and 1.6 × 106 M−1 (Ref. 33 itself) exist. In Ref. 4 there occur values for CO binding to chelated protoheme in 2% phosphate-buffered MTAB solution at pH 7.3 and 20°C of 7.2 × 108 derived from k on, = 3.6 × 106 M−1 s−1 and k off = 0.005 s−1 (Table III referring to Ref. 33 where these values may indeed be located; error ± 10%) and of 4 × 108 (Table I, referring to Ref. 29; from k on = 3.6(1) × 106 M−1 s−1 and koff = 0.0089 s−1). The value for k off may come from Table VI in Ref. 32 for a cetyltrimethylammoniumbromide, CTAB (1.6%), and MTAB (0.4%) mixture. A value of 0.0079 s−1 (error ± 10%) in a 2% CTAB suspension may also be found in Table IV of Ref. 32. From a probable value for the CO solubility in benzene (9.97 × 10−6 M/Torr28), the value for K CO of 4 × 108 M−1 by the chelated protoheme in benzene at 20°C reported in Ref. 4 (which probably originates from Ref. 28) yields a value of 0.00025 Torr. (The stated value is 0.0004). We hope that we have chosen the intended values for inclusion in our Tables I and III.
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  • For chelated protoheme Vb, K co (M−1) = 4.8 × 108 M−1, derived from kinetic measurements in benzene at 20°C.28 For the deuteroheme species derived from IVC with an imidazole base Kco(M−1) = 4.8 × 108 M−1, measured directly in benzene at 25°C (estimated error to ± 30%).42 However, given the different heme and the estimated errors agreement to within only an order of magnitude is demonstrated here. For Cu-Fe cofacial diporphynns43 values for P1/2 measured kinetically and thermodynamically agree within 20%. Comparable data for CO binding, where a second base-off pathway may complicate data analysis, are not available. In a number of picket-fence porphyrin systems equilibrium for ligand binding has been approached from both sides (B. Iverson, personal communication). This approach certainly increases precision and possibly accuracy as well. Ideally we would like to see measurements duplicated in different laboratories, analogous to those frequently encountered in the literature on hemoglobins. This would provide greater confidence in the accuracy of the measurements.
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  • Coordinates from the structure of Fe(TpivPP)(1-Melm)(CO)6 remain unpublished.
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