Dimetallic hydrolases and their models.
Recent mechanistic studies of Fe3+/M2+ purple acid phosphatase present conflicting pictures about the roles of the metals. Recent model studies with Co3+/Co3+ and Fe3+/Fe3+ complexes have supported each conflicting mechanism for phosphate hydrolysis. With dizinc and trizinc complexes, the competitive binding of hydroxyl and phosphate substrates has been demonstrated.
Kimura
E
E
Department of Medicinal Chemistry, Faculty of Medicine, Hiroshima University, Japan. ekimura@ipc.hiroshima-u.ac.jp
D000135:Acid Phosphatase / Q000737:chemistry / Q000378:metabolism; D003035:Cobalt / Q000378:metabolism; D006867:Hydrolases / Q000737:chemistry* / Q000378:metabolism*; D007501:Iron / Q000378:metabolism; D008667:Metalloproteins / Q000737:chemistry* / Q000378:metabolism*; D008670:Metals / Q000378:metabolism*; D008956:Models, Chemical
D008667:Metalloproteins; D008670:Metals; D003035:Cobalt; D007501:Iron; D006867:Hydrolases; D000135:Acid Phosphatase