J. Bacteriol., 01 1997, 290-292, Vol 179, No. 1
Copyright © 1997, American Society for Microbiology

HupUV proteins of Rhodobacter capsulatus can bind H2: evidence from the H-D exchange reaction

PM Vignais, B Dimon, NA Zorin, A Colbeau and S Elsen
CEA/Grenoble, Laboratoire de Biochimie Microbienne (Centre National de la Recherche Scientifique Unite de Recherche Associee no. 1130)/Departement de Biologie Moleculaire et Structurale, France. pmv@miage.ceng.cea.fr

The H-D exchange reaction has been measured with the D2-H2O system, for Rhodobacter capsulatus JP91, which lacks the hupSL-encoded hydrogenase, and R. capsulatus BSE16, which lacks the HupUV proteins. The hupUV gene products, expressed from plasmid pAC206, are shown to catalyze an H-D exchange reaction distinguishable from the H-D exchange due to the membrane-bound, hupSL-encoded hydrogenase. In the presence of O2, the uptake hydrogenase of BSE16 cells catalyzed a rapid uptake and oxidation of H2, D2, and HD present in the system, and its activity (H- D exchange, H2 evolution in presence of reduced methyl viologen [MV+]) depended on the external pH, while the H-D exchange due to HupUV remained insensitive to external pH and O2. These data suggest that the HupSL dimer is periplasmically oriented, while the HupUV proteins are in the cytoplasmic compartment.

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