Abstract
Measurements of oxidation rates, respiratory quotients (RQ), and release of (14)CO(2) from uniformly labeled substrates showed that glutamate, alpha-ketoglutarate, and synthetic and natural amino acid mixtures are oxidized by suspensions of Bdellovibrio bacteriovorus strain 109J. The oxidation of these substrates largely suppress the endogenous respiration of the Bdellovibrio cells and may or may not cause a small increase, 20 to 50%, in their rate of oxygen consumption. The failure of respired substrates to increase markedly the respiration rate of the Bdellovibrio cells over the endogenous value is discussed. Carbon from these substrates is incorporated into the Bdellovibrio cells during oxidation. Acetate is also oxidized, but its oxidation inhibits endogenous respiration by only about 40% and no acetate is assimilated. The RQ of the Bdellovibrio cells changes from a value characteristic of endogenous respiration to that characteristic of the oxidation of glutamate or of a balanced amino mixture very shortly after the attack of the Bdellovibrio cells on their prey, and the latter RQ is maintained during intraperiplasmic growth. Glutamate, or a mixture of amino acids in the external environment, contributes to the carbon dioxide produced by the Bdellovibrio cells growing intraperiplasmically. It is concluded from these data that amino acids, derived from the breakdown of the protein of the prey, serve as a major energy source during intraperiplasmic growth of B. bacteriovorus 108J. Insofar as they were tested, B. bacteriovorus strains 109D and A. 3. 12 were similar in respiration to strain 109J.
MeSH Terms
Acetates/metabolism
Amino Acids/metabolism
Bacteria/growth & development,metabolism
Carbon Isotopes
Chloramphenicol/pharmacology
Escherichia coli
Glutamates/metabolism
Ketoglutaric Acids/metabolism
Oxidation-Reduction
Oxygen Consumption/drug effects
Streptomycin/pharmacology
Chemicals
Acetates
Amino Acids
Carbon Isotopes
Glutamates
Ketoglutaric Acids
Chloramphenicol
Streptomycin
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Hespell R B
Rosson R A
Thomashow M F
Rittenberg S C
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