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. Author manuscript; available in PMC: 2008 Sep 22.

Published in final edited form as: Biochemistry. 2007 Jun 20;46(28):8263–8272. doi: 10.1021/bi700623u

Table 1.

Spectroscopic Properties for rCcP and Its Charge-Reversal Mutants.^a

	pH 6.0				pH 7.5
Mutant	λ_protein (nm)	λ_Soret (nm)	RZ^b	A_Soret/A₃₈₀	λ_Soret (nm)	A_Soret/A₃₈₀
yCcP^c	282	408	1.28 ± 0.03	1.52 ± 0.04	409	1.60 ± 0.04
CcP(MI)^c	282	408	1.28 ± 0.04	1.53 ± 0.02	410	1.67 ± 0.03
rCcP	282	408	1.31	1.54	409	1.62
Negative Cluster Mutants
R31E	281	407	1.40	1.53	410	1.78
E32K	282	409	1.29	1.58	409	1.62
D33K	282	409	1.29	1.60	410	1.69
D34K	282	408	1.29	1.57	408	1.63
E35K	282	408	1.30	1.58	408	1.64
D37K	283	411	1.34	2.23	414	2.59
Mutants Near Ala-193
E201K	280	409	0.73	1.60	410	1.75
E209K	280	409	1.22	1.87	411	2.12
D210K	281	409	1.27	1.71	411	1.93
Mutants Near Glu-290
E118K	279	409	1.12	1.62	410	1.76
E290K	281	407	1.26	1.57	410	1.84
E291K	281	408	1.23	1.53	411	1.87
Top Front-Face Mutants
E17K	280	408	1.22	1.61	411	2.00
D18K	281	408	1.28	1.60	410	1.74
E98K	281	408	1.31	1.55	409	1.62

^a

Absorbance values were obtained at 1 nm intervals between 240 and 700 nm in 0.10 M ionic strength, potassium phosphate buffers.

^b

RZ is the purity number, the ratio of the absorbance at the Soret maximum relative to the absorbance at the maximum of the protein band near 280 nm.

^c

Data from studies reported in references (39, 44).