Structural studies of modified cytochromes c by nuclear magnetic resonance spectroscopy

K. Wüthrich*, I. Aviram, A. Schejter

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

37 Scopus citations


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.

Original languageEnglish
Pages (from-to)98-103
Number of pages6
JournalBiochimica et Biophysica Acta - Bioenergetics
Issue number1
StatePublished - 2 Nov 1971


FundersFunder number
Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung3.378.7o


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