1887

Abstract

A mercuric ion-reducing flavoprotein was purified from TFI 29 by using dye-matrix affinity chromatography. The isolated enzyme had a molecular weight of 130000 and was composed of two subunits (54000 and 62000). The visible absorbance spectrum of the oxidized enzyme had a maximum at 455 nm. Upon addition of NADPH a new absorbance at 540 nm appeared, which was attributed to a charge transfer complex. The for mercuric chloride was determined to be 8·9 and the enzyme was shown to have a turnover number of 746 min per FAD. A comparison of these physical properties, as well as metal ion inhibition and pH profiles, indicate that the enzyme from is very similar in structure and function to mercuric reductases isolated from other bacterial sources.

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1984-03-01
2021-07-25
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