Author's Organization：Faculty of Pharmaceutical Sciences, Kyushu University:(Present address)Central Research Division, Takeda Chemical Industries, Ltd. Faculty of Pharmaceutical Sciences, Kyushu University Institute of pharmaceutical Sciences, Hiroshima University School of Medicine
The properties of oxygen-insensitive nitrofuran reductase from Escherichia coli B/r were investigated by using cell-free preparations. Both the reduced nicotinamide-adenine dinucleotide phosphate (NAD (P) H)-linked and the NADPH-linked nitrofuran reductases are flavoenzymes containing riboflavin 5'-phosphate as a prosthetic group. The former enzyme appears to be a kind of NAD (P) H-linked menadione reductase.
