TY - JOUR
T1 - The role of the lysines in the alkaline heme-linked ionization of ferric cytochrome c
AU - Pettigrew, Graham W.
AU - Aviram, Irit
AU - Schejter, Abel
PY - 1976/2/9
Y1 - 1976/2/9
N2 - Fully amidinated cytochrome c has a 695 nm band which is lost with a pK of 9.2 in a transition to a low-spin state. Fully maleylated cytochrome c can also exist in a low-spin state without the 695 nm band although the pH of the transition is very dependent on the salt concentration. Neither of these derivatives have free lysine groups. It is concluded that the hemelinked alkaline ionization of native cytochrome c is not triggered by deprotonation of a lysine residue, and that lysine does not necessarily coordinate the iron in the low-spin alkaline species.
AB - Fully amidinated cytochrome c has a 695 nm band which is lost with a pK of 9.2 in a transition to a low-spin state. Fully maleylated cytochrome c can also exist in a low-spin state without the 695 nm band although the pH of the transition is very dependent on the salt concentration. Neither of these derivatives have free lysine groups. It is concluded that the hemelinked alkaline ionization of native cytochrome c is not triggered by deprotonation of a lysine residue, and that lysine does not necessarily coordinate the iron in the low-spin alkaline species.
UR - http://www.scopus.com/inward/record.url?scp=0017285861&partnerID=8YFLogxK
U2 - 10.1016/0006-291X(76)91217-1
DO - 10.1016/0006-291X(76)91217-1
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AN - SCOPUS:0017285861
SN - 0006-291X
VL - 68
SP - 807
EP - 813
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 3
ER -