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. Author manuscript; available in PMC: 2008 Sep 29.
Published in final edited form as: Biochemistry. 2006 Dec 5;45(48):14371–14378. doi: 10.1021/bi061662p

Figure 4.

Figure 4

Variation of KM (solid circles) for the V5C/K79C covalent complex as a function of ionic strength. Published data are included for reference. The lower linear plot includes published values for KD1 (open circles) for the yeast iso-1 cytochrome c/CcP complex. The KD1 values include data collected between 18 and 200 mM ionic strength, between pH 5.5 and 7.0, and for complexes formed using either ferri- or ferrocytochrome c (11–13). Michaelis constants for the high-affinity phase, KM1 (open triangles), of the steady-state oxidation of yeast iso-1 ferrocytochrome c catalyzed by yCcP (19) and CcP(MI) (23) are included. The upper linear plot includes values for KD2 (open squares) obtained between 1.8 mM and 118 mM ionic strength, between pH 6 and 7, using proton uptake measurements (11) and dynamic fluorescence quenching of zinc-modified CcP (7, 14, 15). Michaelis constants for the low-affinity phase, KM2 (open diamonds), of the steady-state oxidation of yeast iso-1 ferrocytochrome c catalyzed by yCcP (19) and CcP(MI) (23) are included.