Table 2.

Binding parameters derived from ITC measurements

Data sets for oxidized and reduced proteins were analyzed with either one or two sets of binding sites. Standard deviations were determined from three independent measurements (n, number of binding sites; K_D, dissociation constant; ΔH, binding enthalpy).

	Cyt cHH oxidized		Cyt cHH reduced		Cyt c6 reduced
	1a	2a	1a	2a	1a
n1	1.5 ± 0.1	1b	1.5 ± 0.2	1b	1b
KD1 (μm)	18.8 ± 0.2	11b	24.8 ± 1.2	11b	21 ± 3
ΔH1 (cal/mol)	5320 ± 70	8500 ± 280	4530 ± 250	7290 ± 360	−1370 ± 40
n2		2.0 ± 0.2		6.4 ± 1.2
KD2 (μm)		28.4 ± 1.0		39.4 ± 5.4
ΔH2 (cal/mol)		−480 ± 120		−220 ± 100

^a Number of types of binding sites presumed in the fit.

^b n₁ and K_D1 were set to 1 and 11 μm, respectively, as derived from Michaelis–Menten kinetics.