The role of tryptophanyl residues in electron transfer from NADPH--adrenodoxin reductase to adrenodoxin.
Chemical modification of tryptophanyl residues of NADPH - adrenodoxin reductase by N - bromosuccinimide and trichloroethanol prevents the interaction of the enzyme with adrenodoxin. The modification does not touch other amino acid residues besides tryptophan (tyrosine, lysine and cysteine) or disturb the structure of protein. The presence of adrenodoxin suppresses the modification. The data obtained indicate the participation of adrenodoxin reductase tryptophan residues in the interaction with adrenodoxin.
Sarkissova
Y G
YG
Institute of Biochemistry, Academy of Sciences of Armenian SSR, Yerevan, USSR.
Mardanian
S S
SS
Haroutunian
A V
AV
D000302:Adrenal Cortex / Q000201:enzymology; D000325:Adrenodoxin / Q000378:metabolism*; D001974:Bromosuccinimide / Q000378:metabolism; D003574:Cytochrome c Group / Q000378:metabolism; D004579:Electron Transport; D005023:Ethylene Chlorohydrin / Q000031:analogs & derivatives / Q000378:metabolism; D005287:Ferredoxin-NADP Reductase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D010084:Oxidation-Reduction; D013053:Spectrophotometry; D014364:Tryptophan / Q000737:chemistry*
D003574:Cytochrome c Group; D000325:Adrenodoxin; D005023:Ethylene Chlorohydrin; D014364:Tryptophan; C005849:2,2,2-trichloroethanol; D005287:Ferredoxin-NADP Reductase; D001974:Bromosuccinimide