The role of lysines in Euglena cytochrome c-552. Chemical modification studies

Irit Aviram*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

4 Scopus citations

Abstract

Cytochrome c-552 of Euglena gracilis was modified by transamination of the terminal amino groups and by acetylation and maleylation of α- and ε{lunate}-amino groups. The properties of the derivatives were studied with respect to their optical spectra, hemelinked ionizations, reductions with ascorbate, redox potential, and ability to participate in light-dependent electron transfer. Transaminated cytochrome c-552 resembled the native protein. Acetylation and maleylation did not lead to marked conformation changes but altered the crevice structure. At alkaline pH, acetylated and maleylated cytochrome c-552 existed in a mixed spin form. Both the reduction rates with ascorbate as well as the light-dependent oxidation rates were lowered by these modifications.

Original languageEnglish
Pages (from-to)199-207
Number of pages9
JournalArchives of Biochemistry and Biophysics
Volume181
Issue number1
DOIs
StatePublished - May 1977

Funding

FundersFunder number
United States-Israel Binational Science Foundation

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