Anaerobic adaptation ofParacoccus denitrificans: Sequential formation of denitrification pathway and changes in activity of 5-aminolevulinate synthase and catalase

Kučera, Igor; Matyášek, Roman; Dvořáková, Jiřina; Dadák, Vladimír

doi:10.1007/bf01568291

Cited by 12 publications

(5 citation statements)

References 16 publications

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“…The considerably high concentrations of NO 2 Ϫ in our cultures were probably caused by the delay of expression of nitrite reductase mRNA and, consequently, a delay of synthesis of this enzyme. Retarded induction of nitrite reductase compared with the induction of nitrate reductase has been reported by others (21). The very low levels of NO measured indicate that the expression and synthesis of nitric oxide reductase were not delayed with regard to the expression and synthesis of the nitrite reductase.…”

Section: Discussionsupporting

confidence: 72%

Dynamics of denitrification activity of Paracoccus denitrificans in continuous culture during aerobic-anaerobic changes

et al. 1996

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Induction and repression of denitrification activity were studied in a continuous culture of Paracoccus denitrificans during changes from aerobic to anaerobic growth conditions and vice versa. The denitrification activity of the cells was monitored by measuring the formation of denitrification products (nitrite, nitric oxide, nitrous oxide, and dinitrogen), individual mRNA levels for the nitrate, nitrite, and nitrous oxide reductases, and the concentration of the nitrite reductase enzyme with polyclonal antibodies against the cd 1 -type nitrite reductase. On a change from aerobic to anaerobic respiration, the culture entered an unstable transition phase during which the denitrification pathway became induced. The onset of this phase was formed by a 15-to 45-fold increase of the mRNA levels for the individual denitrification enzymes. All mRNAs accumulated during a short period, after which their overall concentration declined to reach a stable value slightly higher than that observed under aerobic steady-state conditions. Interestingly, the first mRNAs to be formed were those for nitrate and nitrous oxide reductase. The nitrite reductase mRNA appeared significantly later, suggesting different modes of regulation for the three genes. Unlike the mRNA levels, the level of the nitrite reductase protein increased slowly during the anaerobic period, reaching a stable value about 30 h after the switch. All denitrification intermediates could be observed transiently, but when the new anaerobic steady state was reached, dinitrogen was the main product. When the anaerobic cultures were switched back to aerobic respiration, denitrification of the cells stopped at once, although sufficient nitrite reductase was still present. We could observe that the mRNA levels for the individual denitrification enzymes decreased slightly to their aerobic, uninduced levels. The nitrite reductase protein was not actively degraded during the aerobic period.

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Section: Discussionsupporting

confidence: 72%

Dynamics of denitrification activity of Paracoccus denitrificans in continuous culture during aerobic-anaerobic changes

et al. 1996

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“…Levels of cytochromes a and b in membranes were increased to a similar extent (Fig. 4B) (29,56) and is supported by the observation that the levels of membranebound cytochromes in choline-grown DP104 are somewhat lower than those observed in DP104 grown on succinate (see above); presumably the increased synthesis of soluble cytochromes associated with growth on choline further depletes the already reduced pool of heme available for membrane cytochrome assembly. The observation that levels of a-and b-type cytochromes are diminished to similar extents in DP104 indicates that synthesis of heme a is not impaired in spite of the limited availability of protoheme IX.…”

Section: Resultssupporting

confidence: 53%

Differential reduction in soluble and membrane-bound c-type cytochrome contents in a Paracoccus denitrificans mutant partially deficient in 5-aminolevulinate synthase activity

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Ferguson

1994

J Bacteriol

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A mutant of Paracoccus denitrificans, DP104, unable to grow anaerobically with nitrate as the terminal electron acceptor or aerobically with methanol as the electron donor and staining negatively in the dimethylphenylene diamine oxidation (Nadi) test, was isolated by transposon Tn5::phoA mutagenesis. P. denitrificans DP104 grown aerobically with succinate or choline had very low levels (2 to 3% of the wild-type levels) of spectroscopically detectable soluble c-type cytochromes. In contrast, membrane cytochromes of the a, b, and c types were present at 50% of the levels found in the wild type. The apo form of cytochrome c550, at an approximately 1:1 molar ratio with the holo form, was found in the periplasm of DP104. The TnphoA element was shown to be inserted immediately upstream of the translational start of hemA, the gene coding for 5-aminolevulinate synthase, which was sequenced. Low-level expression of this gene, driven off an incidental promoter provided by TnphoA-cointegrated suicide vector DNA, is the basis of the phenotype which could be complemented by the addition of 5-aminolevulinate to growth media. Disruption of the hemA gene generated a P. denitrificans strain auxotrophic for 5-aminolevulinate, establishing that there is no hemA-independent pathway of heme synthesis in this organism. The differential deficiency in periplasmic c-type cytochromes relative to membrane cytochromes in DP104 is suggested to arise from unequal competition for the restricted supply of heme which results from the effects of the transposon insertion.

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“…and appear to have kinetics similar to the expression of denitrification enzymes and soluble cytochromes observed under the same conditions(KUCERA et al 1986). The ability of P. activity of P .…”

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confidence: 54%

Cytochromes c‐dependent aerobic respiration of Paracoccus denitrificans

Kučera

1993

J. Basic Microbiol.

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Terminal parts of the respiratory chain of Paracoccus denitrificans containing cytochromes c have been investigated through the use of NNN′Nprime;‐tetramethyl‐p‐phenylenediamine (TMPD) as an electron donor. The cells have been shown to possess two major membrane bound TMPD oxidases characterized by their different sensitivities to cyanide. The more sensitive one, identified as cytochrome aa3, appears to be produced under oxygen‐rich growth conditions, whereas a less sensitive and as yet uncharacterized enzyme accompanied with only moderate amounts of cytochrome aa3 functions when oxygen becomes limiting. The soluble periplasmic cytochrome cd1 does not contribute significantly to the total oxygen consumption rate, although its maximal catalytic capacity may be high. The fact thap the activity of alternative TMPD oxidase is not proportional to cytochrome o content is discussed in relation to possible occurrence of two distinct cytochrome o‐type terminal oxidases.

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Anaerobic adaptation ofParacoccus denitrificans: Sequential formation of denitrification pathway and changes in activity of 5-aminolevulinate synthase and catalase

Cited by 12 publications

References 16 publications

Dynamics of denitrification activity of Paracoccus denitrificans in continuous culture during aerobic-anaerobic changes

Dynamics of denitrification activity of Paracoccus denitrificans in continuous culture during aerobic-anaerobic changes

Differential reduction in soluble and membrane-bound c-type cytochrome contents in a Paracoccus denitrificans mutant partially deficient in 5-aminolevulinate synthase activity

Cytochromes c‐dependent aerobic respiration of Paracoccus denitrificans

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