Premium
CYTOCHROME P‐450/420 IN PLANT PLASMA MEMBRANES: A POSSIBLE COMPONENT OF THE BLUE‐LIGHT‐REDUCIBLE FLAVOPROTEIN‐CYTOCHROME COMPLEX *
Author(s) -
Kjellbom Per,
Larsson Christer,
Askerlund Per,
Schelin Cecilia,
Widell Susanne
Publication year - 1985
Publication title -
photochemistry and photobiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.818
H-Index - 131
eISSN - 1751-1097
pISSN - 0031-8655
DOI - 10.1111/j.1751-1097.1985.tb01647.x
Subject(s) - cytochrome , chemistry , membrane , hemeprotein , cytochrome b , heme , cytochrome c , coenzyme q – cytochrome c reductase , dimer , biochemistry , photochemistry , organic chemistry , mitochondrion , enzyme , mitochondrial dna , gene
— Carbon monoxide difference spectra and pyridine binding spectra indicate the presence of cytochrome P‐450/420 in plasma membranes from cauliflower inflorescences. Mild lithium dodecylsulfate polyacrylamide gel electrophoresis shows only one heme staining band in the plasma membrane fraction at an apparent molecular weight of 93 kiloDalton. This band is suggested to be due to a cytochrome P‐450/420 dimer, in view of the known molecular weights of animal cytochromes P‐450/420. The plasma membrane‐bound cytochrome P‐450/420 is probably identical to the blue‐light‐reducible b‐type cytochrome of plant plasma membranes, which has been inferred to have a role in photomorphogenesis.