Glucose Dehydrogenase of Bacterium Anitratum: an Enzyme with a Novel Prosthetic Group.

Glucose dehydrogenase of Bacterium anitratum catalyzes the reduction by glucose and other aldoses of dyes such as 2,6-dichlorophenol indophenol and phenazine methosulfate without the intervention of pyridine or flavin nucleotides (2, 3). The primary hydrogen acceptor is a group that is linked to the protein and revealed by a broad absorption band in the near ultraviolet in the oxidized state, a band which upon addition of glucose is replaced by a sharper band with maximum at 337 rnp (4). In order to throw further light on the nature of this prosthetic group, it was necessary to improve the isolation procedure for the enzyme. The present paper describes the modified procedure and presents observations on the properties of the prosthetic group, in situ and in isolation.