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Measurement of the oxidation‐reduction potentials of amicyanin and c ‐type cytochromes from Paracoccus denitrificans
Author(s) -
Gray Kevin A.,
Knaff David B.,
Husain Mazhar,
Davidson Victor L.
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)81496-x
Subject(s) - paracoccus denitrificans , chemistry , cytochrome c , cytochrome c oxidase , cytochrome , biochemistry , periplasmic space , enzyme , mitochondrion , escherichia coli , gene
The oxidation‐reduction potentials of four periplasmic electron carrier proteins from Paracoccus denitrificans have been determined. Their midpoint potentials are: amicyanin, 294±6 mV; cytochrome c ‐550, 253±5 mV; cytochrome c ‐551i, 190±4 mV, and cytochrome c ‐553i, 148±5 mV. Although rapid amicyanin‐mediated transfer of electrons from methylamine dehydrogenase to cytochrome c ‐551i was observed, reduced amicyanin did not reduce oxidized cytochrome c ‐551i in the absence of methylamine dehydrogenase.