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. 2004 Sep;87(3):1939–1950. doi: 10.1529/biophysj.104.042119

TABLE 2.

Frequencies of the νFe-CO and νC-O lines of various NOS, P450cam, and chloroperoxidase (CPO)

Frequency (cm−1)
Protein No. νFe-CO (13C18O) δFe-C-O (13C18O) νC-O (13C18O) Reference
SANOS 1 482 (470)* 560 (543) 1949 (1857) This work
2 497 (481)* 1930 (1843)
SANOS/Arg 3 504 (496) 567 (548) 1917 (1830) This work
nNOS/H4B 4 487 (∼477) 562 (544) 1949 (1856) A
5 501 (∼491) 1930 (1837)
nNOS/H4B/Arg 6 503 (493) 565 (546) 1929 (1841) A
iNOS/H4B 479 560 (550) 1945 (1846)§ B
499
iNOS/H4B/Arg 7 512 (499) 567 (551) 1906 (1819) B
eNOS/H4B/Arg 512 567 N.D. B
P450cam (substrate-free) 8 464 556 1963 C
P450cam/camphor 9 481 558 1940 C
CPO pH 6.1 14 485 (474) 560 (538) 1957.5 (1872) A

Numbers in “No.” column refer to data points in Fig. 7. In “Reference” column, A, Wang et al. (1997); B, Fan et al. (1997); C, Uno et al. (1985) and Wells et al. (1992).

*

The best fit to the data for the deconvolution of the broad 489 cm−1 band with 12C16O identifies a line at 482 cm−1 that we assign to a νFe-CO mode and a line at 497 cm−1 that we assign as a νFe-CO mode plus a less intense heme mode at 498 cm−1. This assignment is confirmed with deconvolution of the 13C18O spectrum where the broad line centered at 475 cm−1 is resolved in two νFe-CO at 470 cm−1 and 481 cm−1, respectively, and a heme mode at 498 cm−1.

The bending mode is not assigned to one set of νFe-CO and νC-O modes or the other.

The precise position of the bands was obtained from spectral deconvolution.

The undeconvoluted νFe-CO line is centered at 487 cm−1 and shifts to 474 cm−1 with 13C18O.

§

Broad band.