The relation of proton motive force, adenylate energy charge and phosphorylation potential to the specific growth rate and efficiency of energy transduction in Bacillus licheniformis under aerobic growth conditions.

H+/ATP-stoichiometry was inferred: -->H+/ATP = 1.83 +/- 0.52 mu, so that at a given -->H+/O-ratio of four (4), the apparent P/O-ratio (inferred from regression analysis) showed a decline of 2.16 to 1.87 for mu = 0 to mu max (we discuss how more than half of this decline will be independent of any change in internal cell-volume). We propose that the constancy of delta G'p and the decrease in the efficiency of energy-conservation (P/O-value) with increasing mu are a way in which the cells try to cope with an apparent less than perfect coordination between anabolism and catabolism to keep up the highest possible mu with a minimum loss of growth-efficiency. Protease production in nitrogen-limited cultures as compared to glucose-limited cultures, and the difference between the A- and B-type, could not be explained by a different energy-status of the cells. -->
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Substance Nomenclature: 0 (Phosphates)
0 (Protons)
415SHH325A (Adenosine Monophosphate)
61D2G4IYVH (Adenosine Diphosphate)
8L70Q75FXE (Adenosine Triphosphate)
EC 3.4.- (Exopeptidases)
EC 3.4.- (Peptide Hydrolases)
Entry Date(s): Date Created: 19930101 Date Completed: 19930527 Latest Revision: 20190830
Update Code: 20221213
DOI: 10.1007/BF00871725
PMID: 8386914
Autor: Bulthuis BA; Department of Microbiology, Vrije Universiteit, Amsterdam, The Netherlands., Koningstein GM, Stouthamer AH, van Verseveld HW
Jazyk: angličtina
Zdroj: Antonie van Leeuwenhoek [Antonie Van Leeuwenhoek] 1993 Jan; Vol. 63 (1), pp. 1-16.
DOI: 10.1007/BF00871725
Abstrakt: The magnitude of the proton motive force (delta p) and its constituents, the electrical (delta psi) and chemical potential (-Z delta pH), were established for chemostat cultures of a protease-producing, relaxed (rel-) variant and a not protease-producing, stringent (rel+) variant of an industrial strain of Bacillus licheniformis (respectively referred to as the A- and the B-type). For both types, an inverse relation of delta p with the specific growth rate mu was found. The calculated intracellular pH (pHin) was not constant but inversely related to mu. This change in pHin might be related to regulatory functions of metabolism but a regulatory role for pHin itself could not be envisaged. Measurement of the adenylate energy charge (EC) showed a direct relation with mu for glucose-limited chemostat cultures; in nitrogen-limited chemostat cultures, the EC showed an approximately constant value at low mu and an increased value at higher mu. For both limitations, the ATP/ADP ratio was directly related to mu. The phosphorylation potential (delta G'p) was invariant with mu. From the values for delta G'p and delta p, a variable -->H+/ATP-stoichiometry was inferred: -->H+/ATP = 1.83 +/- 0.52 mu, so that at a given -->H+/O-ratio of four (4), the apparent P/O-ratio (inferred from regression analysis) showed a decline of 2.16 to 1.87 for mu = 0 to mu max (we discuss how more than half of this decline will be independent of any change in internal cell-volume). We propose that the constancy of delta G'p and the decrease in the efficiency of energy-conservation (P/O-value) with increasing mu are a way in which the cells try to cope with an apparent less than perfect coordination between anabolism and catabolism to keep up the highest possible mu with a minimum loss of growth-efficiency. Protease production in nitrogen-limited cultures as compared to glucose-limited cultures, and the difference between the A- and B-type, could not be explained by a different energy-status of the cells.
Databáze: MEDLINE
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