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. Author manuscript; available in PMC: 2010 Jun 9.
Published in final edited form as: Biochemistry. 2009 Jun 9;48(22):4881–4894. doi: 10.1021/bi801738j

Table 2.

Selected RR band assignments for the CO and H2S-HbI mutant derivatives.

Protein CO H2S
νFe-CO νc-o ν2 ν3 ν4

WtHbIa 516 1945 1579 1500 1372
rHbI 516 1945 1583 1504, 1470 1374 (87%)b
1356 (13%)
ValE7 504 1962 1580 1501 1372
AsnE7 507 1946 nd nd nd
HisE7 502 1965 1583 1505, 1470 1373 (53%)
532 1930 1356 (47%)
LeuB10 504 1944 1583 1502, 1470 1373 (53%)
1355 (47%)
ValB10 504 1946 1582, 1562 1500, 1470 1372 (32%)
1355 (68%)
TyrB10 541 1925 1583 1503. 1470 1372 (80%)
1354 (20%)
ValE11 514 1944 1581 1502, 1470 1373 (70%)
1355 (30%)
TyrE11 514 1940 1581 1502, 1470 1373 (86%)
1356 (14%)
a

Data taken from reference reference 31.

b

The RR spectra were decomposed using peak fitting software from Grams spectra. The relative intensity of each band was calculated by the ratio of their height to the total relative height. nd, not determined.