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. Author manuscript; available in PMC: 2013 Aug 14.
Published in final edited form as: Biochemistry. 2012 Jul 31;51(32):6360–6370. doi: 10.1021/bi300421z

Table 2.

Experimentally fit rate constants (min−1) for loss of the Cys(thiolate)-ligated heme Soret of Fe(II) R266K hCBS. The loss of the Cys(thiolate)-ligated heme Soret was monitored at at 447 nm for Fe(II) R266K hCBS and was fit to a biexponential decay.

Rate of Cys52 Ligand Loss (min−1)
37°Ca 30°C 20°C 10°C
k1 (9 ± 1.1) × 10−2 (5 ± 1.4) × 10−2 (1.4 ± 0.1) × 10−2 (9.1 ± 0.5) × 10−3
k2 (1.2 ± 0.5) × 100 (6.6 ± 0.8) × 10−1 (2.5 ± 0.3) × 10−1 (1.0 ± 0.3) × 10−1
a

Upon equilibration at physiological temperature (37°C), Fe(II) R266K hCBS exists almost exclusively as the ligand-switched form (424 nm Soret), which prevented the measurement of k1 and k2 at this temperature; reported values were extrapolated from Arrhenius plots of k1 and k2 (Figure S3).