TY - JOUR
T1 - Structural studies of modified cytochromes c by nuclear magnetic resonance spectroscopy
AU - Wüthrich, K.
AU - Aviram, I.
AU - Schejter, A.
N1 - Funding Information:
We would like to thank Prof. R. Schwyzer and Prof. H. Gtinthard for the hospitalitye xtendedt o us at their institutes.F inancialsupport by the Swiss National Science Foundation (Project 3.378.7o ) is gratefully acknowledgedO. ne of us (I.A.) is thankful to E.M.B.0. for a short-termf ellowship.
PY - 1971/11/2
Y1 - 1971/11/2
N2 - The binding of methionine to one of the axial positions of the heme iron in various modified mammalian-type cytochromes c has been studied by nuclear magnetic resonance spectroscopy. The modifications of the protein included formylation of tryptophan, alkylation of methionine, and polymerization by treatment with ethanol. Comparison of the data on methionine coordination with data on the ability of the modified cytochromes c to restore the respiration of cytochrome c-depleted rat liver mitochondria, indicates that the redox carrier properties of cytochrome c are maintained only if methionine is bound to the heme iron in the oxidized and the reduced form.
AB - The binding of methionine to one of the axial positions of the heme iron in various modified mammalian-type cytochromes c has been studied by nuclear magnetic resonance spectroscopy. The modifications of the protein included formylation of tryptophan, alkylation of methionine, and polymerization by treatment with ethanol. Comparison of the data on methionine coordination with data on the ability of the modified cytochromes c to restore the respiration of cytochrome c-depleted rat liver mitochondria, indicates that the redox carrier properties of cytochrome c are maintained only if methionine is bound to the heme iron in the oxidized and the reduced form.
UR - http://www.scopus.com/inward/record.url?scp=0015208486&partnerID=8YFLogxK
U2 - 10.1016/0005-2728(71)90237-4
DO - 10.1016/0005-2728(71)90237-4
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AN - SCOPUS:0015208486
SN - 0005-2728
VL - 253
SP - 98
EP - 103
JO - Biochimica et Biophysica Acta - Bioenergetics
JF - Biochimica et Biophysica Acta - Bioenergetics
IS - 1
ER -