FAD takes electrons from NADH and delivers them to ferrocytochrome b5 with bound Fe3+, which is converted to ferricytochrome b5 with Fe2+. Cytochrome b5-Fe2+ passes the electrons to another enzyme-bound Fe3+ to reduce O2 and form ceramide from dihydroceramide
the desaturation reaction catalyzed by Des1 is presumably initiated by an enzyme-bound iron-oxo species that abstracts specifically the C-4 pro (R)-hydrogen atom from the substrate. FAD takes electrons from NADH and delivers them to ferrocytochrome b5 with bound Fe3+, which is converted to ferricytochrome b5 with Fe2+. Cytochrome b5-Fe2+ passes the electrons to another enzyme-bound Fe3+ to reduce O2 and form ceramide from dihydroceramide
the desaturation reaction catalyzed by Des1 is presumably initiated by an enzyme-bound iron-oxo species that abstracts specifically the C-4 pro (R)-hydrogen atom from the substrate. FAD takes electrons from NADH and delivers them to ferrocytochrome b5 with bound Fe3+, which is converted to ferricytochrome b5 with Fe2+. Cytochrome b5-Fe2+ passes the electrons to another enzyme-bound Fe3+ to reduce O2 and form ceramide from dihydroceramide
the desaturation reaction catalyzed by Des1 is presumably initiated by an enzyme-bound iron-oxo species that abstracts specifically the C-4 pro (R)-hydrogen atom from the substrate. FAD takes electrons from NADH and delivers them to ferrocytochrome b5 with bound Fe3+, which is converted to ferricytochrome b5 with Fe2+. Cytochrome b5-Fe2+ passes the electrons to another enzyme-bound Fe3+ to reduce O2 and form ceramide from dihydroceramide
the desaturation reaction catalyzed by Des1 is presumably initiated by an enzyme-bound iron-oxo species that abstracts specifically the C-4 pro (R)-hydrogen atom from the substrate. FAD takes electrons from NADH and delivers them to ferrocytochrome b5 with bound Fe3+, which is converted to ferricytochrome b5 with Fe2+. Cytochrome b5-Fe2+ passes the electrons to another enzyme-bound Fe3+ to reduce O2 and form ceramide from dihydroceramide