Attachment of CO dehydrogenase to the cytoplasmic membrane is limiting the respiratory rate of Pseudomonas carboxydovorans

Rohde, Martin

doi:10.1016/0378-1097(85)90140-5

Cited by 9 publications

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“…We have shown in this paper that the attachment of CO dehydrogenase to cytoplasmic membranes which occurs in intact bacteria (17) can be mimicked in vitro. It is hoped that future in vitro studies will provide a better understanding of the mechanism determining the attachment of CO dehydrogenase to CMs in situ.…”

Section: Discussionmentioning

confidence: 89%

“…Depending on the growth phase, CO dehydrogenase in P. carboxydovorans can occur in association with the CM or dissolved in the cytoplasm (13,17,18). We have shown in the present paper that CMs contained CO dehydrogenase in two different types of binding.…”

Section: Discussionmentioning

confidence: 99%

“…The enzyme catalyzes the oxidation of CO to CO2 (5) and provides two protons and two electrons (9, 14,15) for the subsequent reduction of an electron acceptor which resides in the cytoplasmic membrane (13,17,18). Cytochrome b561 has been considered a strong candidate for the in vivo electron acceptor, as its redox potential is +40 mV (3, 4) and as it is involved in the CO-insensitive branch of the respiratory chain (for a review, see reference 12).…”

mentioning

confidence: 99%

“…However, respiration rates with CO as electron donor could only be observed with membrane-bound CO dehydrogenase. Immunocytochemical localization employing exponential cells revealed 87% of CO dehydrogenase associated with the inner aspect of the cytoplasmic membrane (CM) and 13% located in the cytoplasm (17,18). When the bacteria entered the stationary growth phase or were disintegrated, more than 50% of the enzyme was released from the CM into the cytoplasm.…”

mentioning

confidence: 99%

“…When the bacteria entered the stationary growth phase or were disintegrated, more than 50% of the enzyme was released from the CM into the cytoplasm. Respiration rates were drastically reduced under such conditions (17). The basis for the association of CO dehydrogenase with the CM in vivo is so far unknown.…”

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confidence: 99%

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Removal of CO dehydrogenase from Pseudomonas carboxydovorans cytoplasmic membranes, rebinding of CO dehydrogenase to depleted membranes, and restoration of respiratory activities

Jacobitz

Meyer

1989

J Bacteriol

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In Pseudomonas carboxydovorans, CO dehydrogenase and hydrogenase were found in association with the cytoplasmic membrane in a weakly bound and a tightly bound pool. The pools could be experimentally distinguished on the basis of resistance to removal by washes in low-ionic-strength buffer. The tightly bound pool of the enzymes could be differentially solubilized under conditions leaving the electron transport system intact and with the nondenaturing zwitterionic detergent 3-(3-cholamidopropyl) dimethylammonio 1-propanesulfonic acid (CHAPS) and the nonionic detergent dodecyl ,B-D-maltoside. In vitro reconstitution of depleted membranes with the corresponding supernatants containing CO dehydrogenase led to binding of the enzyme and to reactivation of respiratory activities with CO. The reconstitution reaction required cations with effectiveness which increased with increasing ionic charge: monovalent (Li'), divalent (Mg2+, Mn2+), or trivalent (Cr3+, La3+). Reconstitution of depleted membranes with CO dehydrogenase was specific for CO-grown bacteria. Cytoplasmic membranes from H2-or heterotrophically grown Pseudomonas carboxydovorans had no affinity for CO dehydrogenase at all, indicating the absence of the physiological electron acceptor of the enzyme, which presumably is cytochrome b561, or another membrane anchor.Carbon monoxide dehydrogenase (CO dehydrogenase) is the key enzyme in CO metabolism of Pseudomonas carboxydovorans and other carboxydotrophic bacteria (for reviews, see references 7, 10-13, and 16). The enzyme catalyzes the oxidation of CO to CO2 (5) and provides two protons and two electrons (9,14,15) for the subsequent reduction of an electron acceptor which resides in the cytoplasmic membrane (13,17,18). Cytochrome b561 has been considered a strong candidate for the in vivo electron acceptor, as its redox potential is +40 mV (3, 4) and as it is involved in the CO-insensitive branch of the respiratory chain (for a review, see reference 12). After ultracentrifugation of crude extracts of P. carboxydovorans, more than 50% of CO dehydrogenase appeared in the soluble fraction (14,15). However, respiration rates with CO as electron donor could only be observed with membrane-bound CO dehydrogenase. Immunocytochemical localization employing exponential cells revealed 87% of CO dehydrogenase associated with the inner aspect of the cytoplasmic membrane (CM) and 13% located in the cytoplasm (17,18). When the bacteria entered the stationary growth phase or were disintegrated, more than 50% of the enzyme was released from the CM into the cytoplasm. Respiration rates were drastically reduced under such conditions (17). The basis for the association of CO dehydrogenase with the CM in vivo is so far unknown.A prerequisite for studying attachment and detachment of CO dehydrogenase to CMs of P. carboxydovorans in vitro was the availability of membranes devoid of CO dehydrogenase activity and of the protein itself. Such membranes should contain the complete and active electron transport system and retain the specific e...

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Section: Discussionmentioning

confidence: 89%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Removal of CO dehydrogenase from Pseudomonas carboxydovorans cytoplasmic membranes, rebinding of CO dehydrogenase to depleted membranes, and restoration of respiratory activities

Jacobitz

Meyer

1989

J Bacteriol

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Microbial growth on carbon monoxide

et al. 1992

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The utilization of carbon monoxide as energy and/or carbon source by different physiological groups of bacteria is described and compared. Utilitarian CO oxidation which is coupled to the generation of energy for growth is achieved by aerobic and anaerobic eu-and archaebacteria. They belong to the physiological groups of aerobic carboxidotrophic, facultatively anaerobic phototrophic, and anaerobic acetogenic, methanogenic or sulfate-reducing bacteria. The key enzyme in CO oxidation is CO dehydrogenase which is a molybdo iron-sulfur flavoprotein in aerobic CO-oxidizing bacteria and a nickel-containing iron-sulfur protein in anaerobic ones. In carboxidotrophic and phototrophic bacteria, the CO-born CO2 is fixed by ribulose bisphosphate carboxylase in the reductive pentose phosphate cycle. In acetogenic, methanogenic, and probably in sulfate-reducing bacteria, CODH/acetyl-CoA synthase directly incorporates CO into acetyl-CoA.In plasmid-harbouring carboxidotrophic bacteria, CO dehydrogenase as well as enzymes involved in CO2 fixation or hydrogen utilization are plasmid-encoded. Structural genes encoding CO dehydrogenase were cloned from carboxidotrophic, acetogenic and methanogenic bacteria. Although they are clustered in each case, they are genetically distinct.Soil is a most important biological sink for CO in nature. While the physiological microbial groups capable of CO oxidation are well known, the type and nature of the microorganisms actually representing this sink are still enigmatic. We also tried to summarize the little information available on the nutritional and physicochemical requirements determining the sink strength. Because CO is highly toxic to respiring organisms even in low concentrations, the function of microbial activities in the global CO cycle is critical.

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Immunocytochemical localization of APS reductase and bisulfite reductase in three Desulfovibrio species

et al. 1988

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IMPORTANT NOTE: You are advised to consult the publisher's version (publisher's PDF) if you wish to cite from it. Please check the document version below. Document VersionPublisher's PDF, also known as Version of record Publication date: 1988 Link to publication in University of Groningen/UMCG research database Citation for published version (APA): Kremer, D. R., Veenhuis, M., Fauque, G., Peck Jr., H. D., LeGall, J., Lampreia, J., ... Hansen, T. A. (1988). Immunocytochemical localization of APS reductase and bisulfite reductase in three Desulfovibrio species. Archives of Microbiology, 150(3). https://doi.org/10.1007/BF00407795 Copyright Other than for strictly personal use, it is not permitted to download or to forward/distribute the text or part of it without the consent of the author(s) and/or copyright holder(s), unless the work is under an open content license (like Creative Commons).Take-down policy If you believe that this document breaches copyright please contact us providing details, and we will remove access to the work immediately and investigate your claim. with APS reductase antibodies resulted in a distribution of gold particles over the cytoplasmic membrane region. The localization of the two enzymes is discussed with respect to the mechanism and energetics of dissimilatory sulfate reduction. Key words:Desulfovibrio -Dissimilatory sulfate reduction -APS reductase -Bisulfite reductase -Enzyme localization -Immunogold labeling Dissimilatory sulfate reduction is carried out by a large variety of bacteria (Hansen 1988;Widdel 1988). Most studies on its mechanism have been confined to bacteria belonging to the genus Desulfovibrio (Peck and LeGall 1982;LeGall and Fauque 1988). Dissimilatory sulfate reduction proceeds as follows:Sulfate is activated by ATP-sulfurylase to adenosine phosphosulfate (APS), which is subsequently reduced to sulfite plus AMP by the enzyme APS reductase (LeGall and Fauque 1988). In D. vulgaris Hildenborough APS reductase is a non-heme iron flavoprotein containing two different subunits, of 72 kD and 20 kD molecular mass, but it has an unknown subunit structure (Bramlett and Peck 1975). Its natural electron donor is not known. APS reductase has been detected in several genera of sulfate-reducing bacteria (Stille and Triiper 1984). Offprint requests to: T. A. HansenThe biochemistry of the reduction of sulfite to sulfide is somewhat controversial. A cyclic route, the so-called trithionate pathway, has been postulated, in which trithionate and thiosulfate are intermediates (Akagi 1981). In this route sulfite is first reduced to trithionate by the enzyme bisulfite reductase. However, strong indications were found that in Desulfovibrio spp. this is not the natural pathway (Chambers and Trudinger 1975;LeGall and Fauque 1988) and that in vivo a direct six electron reduction of sulfite to sulfide by the enzyme bisulfite reductase may occur. Whatever route is functioning, bisulfite reductase plays a key role in the dissimilatory reduction of sulfite. Four classes of bisulfite reductas...

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Attachment of CO dehydrogenase to the cytoplasmic membrane is limiting the respiratory rate of Pseudomonas carboxydovorans

Cited by 9 publications

References 0 publications

Removal of CO dehydrogenase from Pseudomonas carboxydovorans cytoplasmic membranes, rebinding of CO dehydrogenase to depleted membranes, and restoration of respiratory activities

Removal of CO dehydrogenase from Pseudomonas carboxydovorans cytoplasmic membranes, rebinding of CO dehydrogenase to depleted membranes, and restoration of respiratory activities

Microbial growth on carbon monoxide

Immunocytochemical localization of APS reductase and bisulfite reductase in three Desulfovibrio species

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