H-1 NMR studies of the interaction between cytochrome c(3) and ferredoxin I from D-vulgaris Miyazaki F

Heme assignment of the H-1 NMR spectrum of cytochrome c(3) of D. vulgaris M iyazaki F was established [Reference: 12, 13]. The major reduction of the h eme turned out to take place in the other of heme 4, 1, 2 and 3 (in the seq uential numbering). The Hemes with the smallest and greatest solvent access ibility were reduced at the highest and lowest potentials in average, respe ctively. A cooperation interheme interaction was attributed to a pait of th e closest hemes, namely, hemes 1 and 2. This assignment can provide the phy sicochemical bases for the elucidation of electron transfer of this protein .