C. King, S. F. Chang, H. Gutmann
Jun 1, 1963
Citations
0
Influential Citations
11
Citations
Journal
The Journal of biological chemistry
Abstract
III. 2,3-FLUORENOQUINONE FROM 2-AMINO-3-FLUORENOL AND BINDING OF QUINONOID OXIDATION PRODUCTS TO BOVINE SERUM ALBUMIN* H. R. GUTMANN AND H. T. NAGASAWA From the Radioisotope Service, Veterans Administration Hospital, and the Departments of Physiological and Pharmaceutical Chemistry, University of Minnesota, Minneapolis, Minnesota (Received for publication, July 21, 1960) The o-aminophenols, 2-amino-1-fluorenol, 3-hydroxy-4-amino- biphenyl, and o-aminophenol itself, are readily oxidized by cyto- chrome c and rat kidney (or rat liver) mitochondria or by cyto- chrome c and soluble cytochrome oxidase to colored dimeric products which have been identified as indophenols or isophe- noxazones, or both (1, 2). Thii dimerization may be explained satisfactorily by the transitory existence of o-quinoneimmes, the primary oxidation products of o-aminophenols. 2-Imino-1,2- fluorenoquinone, the primary oxidation product of a-amino-l- fluorenol, was found to bind extensively to bovine serum albumin in a model system (1). In the present report the enzymatic oxidation product of 2- amino-3-fluorenol, an o-aminophenol isomeric with a-amino-l- fluorenol, has been identified as 2,3-fluorenoquinone, and evi- dence is presented that the enzymatic oxidation product interacts with bovine serum albumin. 2-Imino-2,3-fluorenoquinone,’ the primary oxidation product of 2-amino-3-fluorenol, which was synthesized and characterized in this study, was also bound to albumin in model experiments.