The membrane-bound hydrogenase of Alcaligenes eutrophus: II. Localization and immunological comparison with other hydrogenase systems.
Immunological comparison of the soluble and the membrane-bound hydrogenase of Alcaligenes eutrophus revealed no common antigenic determinants shared by the native proteins, however, a small amount of cross-reacting material was detected after freezing and thawing. Immune precipitation assays supported previous observations indicating the membrane-bound hydrogenase to be localized in the outer surface of the cytoplasmic membrane. The membrane-bound hydrogenases of A. eutrophus and Pseudomonas pseudoflava showed close immunological relationship, and material cross-reacting to both antisera was found in membrane extracts of all hydrogen-oxidizing strains of Pseudomonas. Alcaligenes and Aquaspirillum. Material cross-reacting to the membrane-bound hydrogenase of Xanthobacter autotraphicus GZ 29 was found only in a few hydrogen-oxidizing bacteria. Material cross-reacting to the soluble hydrogenase of A. eutrophus was detected in strains of A. eutrophus and A. ruhlandii only. Comparison of the membrane-bound hydrogenase of A. eutrophus, P. pseudoflava and X. autotrophicus with hydrogenases of other physiological bacterial groups revealed serological relationship to the membrane-bound hydrogenases of the hydrogen bacteria and of Chromatium vinosum only. The results are discussed in terms of physiological, taxonomical, and evolutionary aspects.
D000421:Alcaligenes / Q000201:enzymology* / Q000648:ultrastructure; D000942:Antigens, Bacterial / Q000032:analysis; D001419:Bacteria / Q000201:enzymology*; D002462:Cell Membrane / Q000201:enzymology; D002844:Chromatium / Q000201:enzymology; D003429:Cross Reactions; D000939:Epitopes; D006864:Hydrogenase; D010088:Oxidoreductases / Q000032:analysis* / Q000276:immunology; D011549:Pseudomonas / Q000201:enzymology
D000942:Antigens, Bacterial; D000939:Epitopes; D010088:Oxidoreductases; D006864:Hydrogenase