Role and oxidation state of the pterin molybdenum cofactor of molybdenum enzymes: studies of a Drosophila melanogaster xanthine dehydrogenase (rosy) variant, G1011E.
Doyle
W A
WA
School of Biological Sciences and Chemistry, University of Sussex, Brighton, U.K.
Chovnick
A
A
Whittle
J R
JR
Bray
R C
RC
D000818:Animals; D003067:Coenzymes / Q000378:metabolism; D003574:Cytochrome c Group; D004331:Drosophila melanogaster / Q000201:enzymology*; D014644:Genetic Variation; D007700:Kinetics; D008667:Metalloproteins / Q000378:metabolism*; D008982:Molybdenum / Q000378:metabolism; D000090006:Molybdenum Cofactors; D009243:NAD / Q000378:metabolism; D010084:Oxidation-Reduction; D011621:Pteridines / Q000378:metabolism*; D014968:Xanthine Dehydrogenase / Q000302:isolation & purification / Q000378:metabolism*
D003067:Coenzymes; D003574:Cytochrome c Group; D008667:Metalloproteins; D008982:Molybdenum; D000090006:Molybdenum Cofactors; D009243:NAD; D011621:Pteridines; D014968:Xanthine Dehydrogenase; C022261:molybdopterin