Changes in the redox state and composition of the quinone pool of Escherichia coli during aerobic batch-culture growth

Bekker, Martijn; Kramer, Gertjan; Hartog, Aloysius F.; Wagner, Marijke J.; Koster, Chris G. de; Hellingwerf, Klaas J.; Mattos, M. Joost Teixeira de

doi:10.1099/mic.0.2007/006098-0

Cited by 78 publications

(90 citation statements)

References 25 publications

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“…-10 mV), considering the distribution values for E. coli reported in the literature. 18 Unfortunately, the actual situation is more complex, since the Fe(II)-citrate system is in equilibrium with the several different complex species. 43 Nonetheless, there seems to be the possibility that microbes change the quinone during reduction.…”

Section: Resultsmentioning

confidence: 99%

“…[15][16][17] Understanding the dynamic behavior of the quinones requires their frequent monitoring; for example, it has been reported that E. coli can control the UQ and MK productions within minutes depending on the oxygen availability. 18 However, their rapid determinations have been difficult due to the laborious analytical procedures consisting of repeated organic solvent extraction and centrifugation, followed by HPLC determination. 1,[18][19][20] To circumvent this problem, we have developed a novel technique based on the adsorption of the microbial quinones on an indium-tin oxide (ITO) electrode simply by drying the microbes (thermal lysis) applied on the electrode (Fig.…”

Section: (Ementioning

confidence: 99%

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Electrochemical Investigation of Isoprenoid Quinone Productions byShewanella oneidensisMR-1 Detected by Its Destructive Adsorption on an Indium-Tin-Oxide Electrode

Morishita

Higashimae

Nomoto

et al. 2016

J. Electrochem. Soc.

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Ubiquinone and menaquinone play important roles in microbial respiratory chains. S. oneidensis is a facultative anaerobe, and it has been known that this microbe requires menaquinone (MK) and/or methylmenaquinone (MMK) to reduce inorganic and organic compounds, such as Fe(III), Mn(IV), fumarate, and nitrate, under anaerobic conditions. In this article, we show that voltammetry is useful to quantify ubiquinone (UQ), MK and MMK located in the cytoplasmic membrane simply by heating the microbe (thermal lysis) deposited on an indium-tin oxide electrode. It was found that the microbe predominantly produced UQ under aerobic conditions, while the production was switched to that of MMK under anaerobic conditions. This transition occurred at a dissolved oxygen concentration of ∼0.3 mg L −1 . It was also found in this study that the total quinone concentration (UQ + MK + MMK) in a single cell was constant at all stages of the culture in a nutrition broth, suggesting that the cytoplasmic membrane was saturated with the quinones. The reduction of Fe(III) citrate with S. oneidensis was also studied. It was found that this microbe decreased the UQ and MMK levels to 45% and 39% of the initial values, respectively, after finishing the reduction.

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Section: Resultsmentioning

confidence: 99%

Section: (Ementioning

confidence: 99%

Electrochemical Investigation of Isoprenoid Quinone Productions byShewanella oneidensisMR-1 Detected by Its Destructive Adsorption on an Indium-Tin-Oxide Electrode

Morishita

Higashimae

Nomoto

et al. 2016

J. Electrochem. Soc.

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“…The naphthoquinone level is significantly up-regulated during the aerobiosis-to-anaerobiosis transition (15)(16)(17), indicating that menaquinone biosynthesis is subject to aeration control. However, the O 2 -dependent Arc, Fnr, and AppY transcriptional regulatory systems have been demonstrated not to regulate the biosynthesis of menaquinone by gene knock-out experiments (18,19).…”

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confidence: 95%

A Bicarbonate Cofactor Modulates 1,4-Dihydroxy-2-naphthoyl-Coenzyme A Synthase in Menaquinone Biosynthesis of Escherichia coli

Jiang

Chen

Guo

et al. 2010

Journal of Biological Chemistry

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1,4-Dihydroxy-2-naphthoyl coenzyme A (DHNA-CoA) synthase is a typical crotonase-fold protein catalyzing an intramolecular Claisen condensation in the menaquinone biosynthetic pathway. We have characterized this enzyme from Escherichia coli and found that it is activated by bicarbonate in a concentration-dependent manner. The bicarbonate binding site has been identified in the crystal structure of a virtually identical ortholog (96.8% sequence identity) from Salmonella typhimurium through comparison with a bicarbonate-insensitive orthologue. Kinetic properties of the enzyme and its site-directed mutants of the bicarbonate binding site indicate that the exogenous bicarbonate anion is essential to the enzyme activity. With this essential catalytic role, the simple bicarbonate anion is an enzyme cofactor, which is usually a small organic molecule derived from vitamins, a metal ion, or a metal-containing polyatomic anionic complex. This finding leads to classification of the DHNA-CoA synthases into two evolutionarily conserved subfamilies: type I enzymes that are bicarbonate-dependent and contain a conserved glycine at the bicarbonate binding site; and type II enzymes that are bicarbonate-independent and contain a conserved aspartate at the position similar to the enzyme-bound bicarbonate. In addition, the unique location of the enzymebound bicarbonate allows it to be proposed as a catalytic base responsible for abstraction of the ␣-proton of the thioester substrate in the enzymatic reaction, suggesting a unified catalytic mechanism for all DHNA-CoA synthases.Menaquinone is a lipid soluble naphthoquinone that plays important biological roles. In many bacterial microorganisms, menaquinone serves as an electron transporter in the respiratory chain and is essential for their survival (1, 2). In humans and animals, menaquinone is a vitamin (K2) and is used as an enzyme cofactor involved in post-translational glutamate ␥-carboxylation of proteins in blood coagulation (3, 4), bone metabolism (5), and calcification of arteries and other soft tissues (6). This naphthoquinone is synthesized from the chorismate of the shikimate pathway in microorganisms (1, 2, 7, 8), whereas it has to be acquired from diet or intestinal microflora in humans or animals (9, 10). Due to its absence in humans and animals, menaquinone biosynthesis has been an attractive target for development of antibiotics against a number of important microbial pathogens, such as Mycobacterium tuberculosis and Staphylococcus aureus (11,12).Menaquinone biosynthesis has been most extensively studied in the facultative anaerobe Escherichia coli that uses the naphthoquinone (MK-8) and its demethylated congener (demethylmenaquinone, DMK-8) as an obligatory electron transporter under anaerobic conditions when the electron acceptor is fumarate, dimethyl sulfoxide, or trimethylamine N-oxide (13,14). The naphthoquinone level is significantly up-regulated during the aerobiosis-to-anaerobiosis transition (15-17), indicating that menaquinone biosynthesis is subject to aerati...

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“…The elution was monitored at 278 nm by using an SPD-M6A photodiode array detector (Shimadzu, Japan). UQ from purified UQ-mGDH samples was identified by comparison of its migration with those of standard UQs (UQ 8 and UQ 6 ), and the content was estimated from the ratio of the peak area to that of the internal standard UQ 6 . The content of MQ from purified MQ samples was determined by correction, with the ratio of the extinction coefficient of MQ to that of UQ, of the values estimated similarly by comparison with that of internal standard UQ 6 .…”

Section: Methodsmentioning

confidence: 99%

“…UQ n as an electron carrier is primarily involved in aerobic respiration, whereas MQ n is involved in anaerobic respiration. Bekker et al (6) reported significant changes in both size and redox state of the Q pool when the environment changes from a well aerated environment to an environment with low oxygen availability. Some respiratory components that intrinsically interact with Q are capable of catalyzing redox reactions with both UQ and MQ (7)(8)(9)(10)(11).…”

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confidence: 99%

Menaquinone as Well as Ubiquinone as a Bound Quinone Crucial for Catalytic Activity and Intramolecular Electron Transfer in Escherichia coli Membrane-bound Glucose Dehydrogenase

Mustafa

Migita

Ishikawa

et al. 2008

Journal of Biological Chemistry

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Escherichia coli membrane-bound glucose dehydrogenase (mGDH), which is one of quinoproteins containing pyrroloquinoline quinone (PQQ) as a coenzyme, is a good model for elucidating the function of bound quinone inside primary dehydrogenases in respiratory chains. Enzymatic analysis of purified mGDH from cells defective in synthesis of ubiquinone (UQ) and/or menaquinone (MQ) revealed that Q-free mGDH has very low levels of activity of glucose dehydrogenase and UQ 2 reductase compared with those of UQ-bearing mGDH, and both activities were significantly increased by reconstitution with UQ 1 . On the other hand, MQ-bearing mGDH retains both catalytic abilities at the same levels as those of UQ-bearing mGDH. A radiolytically generated hydrated electron reacted with the bound MQ to form a semiquinone anion radical with an absorption maximum at 400 nm. Subsequently, decay of the absorbance at 400 nm was accompanied by an increase in the absorbance at 380 nm with a first order rate constant of 5.7 ؋ 10 3 s ؊1 . This indicated that an intramolecular electron transfer from the bound MQ to the PQQ occurred. EPR analysis revealed that characteristics of the semiquinone radical of bound MQ are similar to those of the semiquinone radical of bound UQ and indicated an electron flow from PQQ to MQ as in the case of UQ. Taken together, the results suggest that MQ is incorporated into the same pocket as that for UQ to perform a function almost equivalent to that of UQ and that bound quinone is involved at least partially in the catalytic reaction and primarily in the intramolecular electron transfer of mGDH.Facultative anaerobic bacteria and lower eukaryotes are known to have capabilities to adapt to environmental changes for survival. One such capability is acquired by synthesis of both UQ 2 and MQ(1). A fine control of biosynthesis and the relative concentrations of the two Qs is crucial for growth, in respect to oxygen supply under aerobic and anaerobic conditions (2-5). UQ n as an electron carrier is primarily involved in aerobic respiration, whereas MQ n is involved in anaerobic respiration. Bekker et al.(6) reported significant changes in both size and redox state of the Q pool when the environment changes from a well aerated environment to an environment with low oxygen availability. Some respiratory components that intrinsically interact with Q are capable of catalyzing redox reactions with both UQ and MQ (7-11). Such interactions may be important in physiological and evolutionary aspects in addition to enzymatic function. DsbB, which is involved in the formation of disulfide bonds in Escherichia coli extracytoplasmic space, and fumarate reductase differentially employ Q under aerobic and anaerobic conditions (7-9). The respiratory oxidation in E. coli of ␣-glycerophosphate and D-lactate is promoted by both UQ and MQ, whereas NADH oxidase and succinate oxidase require only UQ for activity (12).E. coli membrane-bound mGDH, which is known as a quinoprotein, catalyzes the oxidation of D-glucose to D-gluconate at the periplas...

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Changes in the redox state and composition of the quinone pool of Escherichia coli during aerobic batch-culture growth

Cited by 78 publications

References 25 publications

Electrochemical Investigation of Isoprenoid Quinone Productions byShewanella oneidensisMR-1 Detected by Its Destructive Adsorption on an Indium-Tin-Oxide Electrode

Electrochemical Investigation of Isoprenoid Quinone Productions byShewanella oneidensisMR-1 Detected by Its Destructive Adsorption on an Indium-Tin-Oxide Electrode

A Bicarbonate Cofactor Modulates 1,4-Dihydroxy-2-naphthoyl-Coenzyme A Synthase in Menaquinone Biosynthesis of Escherichia coli

Menaquinone as Well as Ubiquinone as a Bound Quinone Crucial for Catalytic Activity and Intramolecular Electron Transfer in Escherichia coli Membrane-bound Glucose Dehydrogenase

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