Structure and mechanism of cytosolic quinone reductases.
Department of Biophysics and Biophysical Chemistry, Johns Hopkins Medical School, Baltimore, MD 21205, USA.
M A
MA
Bianchet
C
C
Foster
M
M
Faig
P
P
Talalay
L M
LM
Amzel
D000818:Animals; D016227:Benzoquinones / Q000494:pharmacology; D001665:Binding Sites; D003600:Cytosol / Q000201:enzymology*; D019281:Dimerization; D004583:Electrons; D004791:Enzyme Inhibitors / Q000494:pharmacology; D005182:Flavin-Adenine Dinucleotide / Q000737:chemistry / Q000378:metabolism; D016660:NAD(P)H Dehydrogenase (Quinone) / Q000737:chemistry* / Q000378:metabolism*; D009249:NADP / Q000737:chemistry / Q000378:metabolism; D011487:Protein Conformation; D014227:Triazines / Q000494:pharmacology
D016227:Benzoquinones; D004791:Enzyme Inhibitors; D014227:Triazines; D005182:Flavin-Adenine Dinucleotide; D009249:NADP; C012842:Cibacron Blue F 3GA; D016660:NAD(P)H Dehydrogenase (Quinone); C034257:duroquinone