Tuna ferrocytochrome

A series of exciting papers on cytochrome c by Dickerson et al. includes a report on the structures at 2.8 A resolution of horse and bonito ferricyto-chromes, a speculative discussion on chain flexibility in ferricytochrome, a report of tuna ferrocytochrome at 2.45 A resolution, and a discussion of sequence and structure homologies in bacterial and mammalian-type cytochromes. ... 

Ferricytochrome c outer (tuna) Ferricytochrome c inner (tuna) Ferrocytochrome c (bonito)... 

Fig. 27. The high-frequency shifted portions of the 400 MHz H NMR spectra of ferrocytochromes c in 90%H20/10% H20 at 5 °C. (A) Horse cyt-c, pH 8.75. (A ) Same as (A), but in the presence of 400 mM NaCl. (B) Tuna cyt-c, pH 8.68. Peaks resolved in the region 10-11 ppm of trace A have been assigned. (From ref. 123, 1997, with permission from the publisher.)...

The structures of ferrocytochrome c from tuna (17) and bonito (23) are in essential agreement, and Fig. 9 of ref. 23 shows a stereo comparison of the heme and left channel aromatic ring orientations in these two molecules and in horse ferricytochrome. Because of the poor quality of the horse map, these latter orientations must be considered provisional, and in a sense this chapter is one year premature. A detailed comparison of accurate ring orientations in oxidized and reduced cytochrome will soon be possible, but cannot yet be made. Although the crystal forms obtained... 

Oxidized high-potential iron protein Chromatium vinarum D) Ferrocytochrome c (tuna)... 

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