TABLE 1.

Kinetics of CO binding and dissociation in heme-containing SCHIC domain AppA and PpaA proteins from R. sphaeroides^a

Protein	Constant for CO binding		Equilibrium dissociation constant (μM)
	On rate (μM−1 s−1)	Off rate (s−1)
AppA	1.03 ± 0.02b	0.77 ± 0.09	0.75
PpaA	0.95 ± 0.04	0.70 ± 0.09	0.74

^aMBP-AppA (data from reference 23) and MBP-SCHIC_Rs. Data are means ± standard deviations, determined based on kinetic traces that were recorded at least four times using two independently reconstituted protein samples.