Open AccessCircular dichroic evidence for a conformational change in a cytochrome b--c1 complex by uncoupling agents.
Author(s) -
Jennifer Reed,
Thomas A. Reed,
Benno Hess
Publication year - 1979
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.76.3.1045
Subject(s) - dichroic glass , cytochrome , heme , cytochrome b , crystallography , chemistry , cytochrome c , cytochrome c1 , stereochemistry , conformational change , photochemistry , coenzyme q – cytochrome c reductase , biochemistry , materials science , mitochondrion , nanotechnology , enzyme , mitochondrial dna , gene
Circular dichroic spectra of the cytochrome b--c1 complex exhibit bilobe formation typical of exciton splitting in the presence of uncoupler. Bilobe formation occurs if both cytochrome c1 and cytochrome b are fully reduced. The fully oxidized and ascorbate-reduced complexes are not altered dichroically by uncouplers. The exciton splitting induced by uncoupler is consistent with heme--heme interaction: specifically, interaction between the two cytochromes b in the complex.