Molecular and immunological comparison of membrane-bound, H2-oxidizing hydrogenases of Bradyrhizobium japonicum, Alcaligenes eutrophus, Alcaligenes latus, and Azotobacter vinelandii

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The membrane-bound hydrogenase of Alcaligenes eutrophus. I. Solubilization, purification, and biochemical properties.

The membrane-bound hydrogenase of Alcaligenes eutrophus was solubilized from washed membranes of autotrophically grown cells. The enzyme consists of two types of subunits and is an iron-sulfur protein. A flavin compound was not detected. The enzyme reacts only with few artificial electron acceptors.

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Dissimilation of aromatic compounds by Alcaligenes eutrophus.

The range of aromatic compounds that support the growth of Alcaligenes eutrophus has been determined, and the pathways used for the dissimilation of these substrates have been explored, largely by enzymatic analyses. The beta-ketoadipate pathway operates in the dissimilation of benzoate and p-hydroxybenzoate; the genetisate pathway, in the dissimilation of m-hydroxybenzoate; and the meta cleava...

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Purification of hydrogenases by affinity chromatography on Procion Red-agarose.

The agarose-coupled triazine dye Procion Red HE-3B has been demonstrated to be applicable as an affinity gel for the purification of five diverse hydrogenases, namely the soluble, NAD-specific and the membrane-bound hydrogenase of Alcaligenes eutrophus, the membrane-bound hydrogenase of the N2-fixing Alcaligenes latus, the reversible H2-evolving and the unidirectional H2-oxidizing hydrogenase o...

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Denitrification by Alcaligenes eutrophus is plasmid dependent.

Curing of the hydrogenase-specifying megaplasmid pHG indigenous to strains of the facultative lithoautotrophic bacterium Alcaligenes eutrophus was correlated with a loss of denitrifying ability (Nitd). The retransfer of plasmid pHG1 reconstituted the Nitd phenotype. Plasmid-free mutants were still capable of converting some nitrate to nitrite, but they did not metabolize nitrite under anaerobic...

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Antigenic determinants of the membrane-bound hydrogenase in Alcaligenes eutrophus are exposed toward the periplasm.

Electron microscopic immunogold labeling experiments were performed with ultrathin sections of plasmolyzed cells of Alcaligenes eutrophus and "whole-mount" samples of spheroplasts and protoplasts. They demonstrated that antigenic determinants of the membrane-bound hydrogenase are exposed, at the outside of the cytoplasmic membrane, to the periplasm.

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ژورنال

عنوان ژورنال: Journal of Bacteriology

سال: 1985

ISSN: 0021-9193,1098-5530

DOI: 10.1128/jb.163.1.15-20.1985