Ss. Mardanyan et Eg. Sarkisova, THE INTERACTION OF FLAVIN ADENINE-DINUCLE OTIDE AND TRYPTOPHANE NADFHADRENODOXIN REDUCTASE LOCATED IN COMPLEX WITH ADRENODOXIN, Biofizika, 40(1), 1995, pp. 23-29
The NADFH-adrenodoxin complex with adrenodoxin is responsible for the
transformation of the two-electron flow from NADH to the mono-electron
flow to cytochrome P-450 in the steroid-hydroxil enzyme system of mit
ochondria of kidney crust. Depolarization of emission of the reductase
prostetic group FAD with the maximum at 525 nm excited at the wave le
ngth approximately 290 nm in comparison with the excited at 450 nm pro
vides an evidence of presence of the Ferster energy excitement transfe
r to FAD from the group absorbed at 290 nm. This fact and the form of
absorbance spectra of the complex of two peptide points to the fact th
at the complex formation is accompanied by interaction of FAD with the
residue of tryptophan in the reductase. Based on these facts and the
data concerning participation of tryptophan and tyrosine of adrenodoxi
n in the electron transfer between the hypothesis is suggested about t
he intracomplex path of the electron that can explain the mechanism of
switching of the two-electron transfer into the mono-electron one.