TABLE 1.
Group and signala | Chemical shift (ppm) of signal in oxidation stateb
|
||||
---|---|---|---|---|---|
S0 | S1 | S2 | S3 | S4 | |
Group 1 | |||||
A | 38.50 | 22.20 | 18.10 | 7.40 | 1.60 |
H | 19.30 | 11.00 | 10.20 | ||
I | 17.00 | 10.50 | 8.60 | ||
Group 2 | |||||
C | 30.00 | 19.60 | 5.90 | 3.70 | |
D | 26.90 | 18.50 | 5.85 | 4.15 | |
Group 3 | |||||
F | 22.40 | 18.30 | 12.35 | 7.05 | 0.95 |
G | 21.30 | 19.00 | 18.15 | 9.30 | |
J | 14.30 | 12.40 | 8.80 | 6.80 | |
K | 13.25 | 11.40 | 7.95 | 5.90 | 2.70 |
Group 4 | |||||
B | 35.30 | 34.90 | 32.80 | 19.60 | 3.25 |
E | 23.00 | 22.50 | 20.80 | 13.40 |
The signal labels are given in Fig. 5.
Chemical shifts of heme methyl signals of S. oneidensis small tetraheme cytochrome c in five oxidation states. S0, S1, S2, S3, and S4 stand for the fully oxidized, one-electron reduced, two-electron reduced, three-electron reduced, and fully reduced states, respectively.