Silicate in the Metabolism of Azotobacter vinelandii

Abstract

MOLYBDENUM complexed as silico-molybdate has been shown to be very active in the re-activation of aldehyde oxidase from which the molybdenum has been removed by dialysis¹. Other reports have implicated silicate, phosphate and other anions as agents which increase the activity of molybdate -dependent enzymes^2,3. Jacobs and Sanadi⁴ suggested that a silico-molybdate complex was involved in a terminal electron transport system that was coupled with phosphorylation. It was shown by Glenn and Crane⁵, however, that the in vivo functioning of aldehyde oxidase was probably not dependent on silico-molybdate even though it did greatly enhance the activity of the in vitro system.