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Electron Transport System (electron + transport_system)
Selected AbstractsElectron Transport System (ETS) Activity in Alder Leaf Litter in Two Contrasting Headwater StreamsINTERNATIONAL REVIEW OF HYDROBIOLOGY, Issue 4-5 2007Tadeusz Fleituch Abstract Decomposition rates, carbon and nitrogen concentrations and respiration electron transport (ETS) activity in alder leaf litter were examined by bag exposition method in two contrasting 2nd order streams. Oberer Seebach, Austria (alpine, limestone, karstic) and Goscibia, Poland (sub mountain, flysh) contrasted in catchment geology, channel hydrology, thermal regime and water chemistry. Despite differences in water temperature, the breakdown rates did not show statistical differences. However, the C:N ratio in alder leaf litter varied significantly between two sites. The potential ETS activity was significantly higher in the colder Goscibia and weakly related to stream thermal regimes. The effect of temperature on ETS of alder leaves was not the dominating factor. It was masked by variation of other factors like stream chemistry and the contribution of fine sediments, which are related to stream morphology and channel hydrology. (© 2007 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim) [source] Respiratory protection of nitrogenase in Azotobacter species: is a widely held hypothesis unequivocally supported by experimental evidence?FEMS MICROBIOLOGY REVIEWS, Issue 4 2000Jürgen Oelze Abstract The hypothesis of respiratory protection, originally formulated on the basis of results obtained with Azotobacter species, postulates that consumption of O2 at the surface of diazotrophic prokaryotes protects nitrogenase from inactivation by O2. Accordingly, it is assumed that, at increased ambient O2 concentrations, nitrogenase activity depends on increased activities of a largely uncoupled respiratory electron transport system. The present review compiles evidence indicating that cellular O2 consumption as well as both the activity and the formation of the respiratory system of Azotobacter vinelandii are controlled by the C/N ratio, that is to say the ratio at which the organism consumes the substrate (i.e. the source of carbon, reducing equivalents and ATP) per source of compound nitrogen. The maximal respiratory capacity which can be attained at increased C/N ratios, however, is controlled, within limits, by the ambient O2 concentration. When growth becomes N-limited at increased C/N ratios, cells synthesize nitrogenase and fix N2. Under these diazotrophic conditions, cellular O2 consumption remains constant at a level controlled by the O2 concentration. Control by O2 has been studied on the basis of both whole cell respiration and defined segments of the respiratory electron transport chain. The results demonstrate that the effect of O2 on the respiratory system is restricted to the lower range of O2 concentrations up to about 70 ,M. Nevertheless, azotobacters are able to grow diazotrophically at dissolved O2 concentrations of up to about 230 ,M indicating that respiratory protection is not warranted at increased ambient O2 concentrations. This conclusion is supported and extended by a number of results largely excluding an obvious relationship between nitrogenase activity and the actual rate of cellular O2 consumption. On the basis of theoretical calculations, it is assumed that the rate of O2 diffusion into the cells is not significantly affected by respiration. All of these results lead to the conclusion that, in the protection of nitrogenase from O2 damage, O2 consumption at the cell surface is less effective than generally assumed. It is proposed that alternative factors like the supply of ATP and reducing equivalents are more important. [source] Characterization of CetA and CetB, a bipartite energy taxis system in Campylobacter jejuniMOLECULAR MICROBIOLOGY, Issue 5 2008Kathryn T. Elliott Summary The energy taxis receptor Aer, in Escherichia coli, senses changes in the redox state of the electron transport system via an flavin adenine dinucleotide cofactor bound to a PAS domain. The PAS domain (a sensory domain named after three proteins Per, ARNT and Sim, where it was first identified) is thought to interact directly with the Aer HAMP domain to transmit this signal to the highly conserved domain (HCD) found in chemotaxis receptors. An apparent energy taxis system in Campylobacter jejuni is composed of two proteins, CetA and CetB, that have the domains of Aer divided between them. CetB has a PAS domain, while CetA has a predicted transmembrane region, HAMP domain and the HCD. In this study, we examined the expression of cetA and cetB and the biochemical properties of the proteins they encode. cetA and cetB are co-transcribed independently of the flagellar regulon. CetA has two transmembrane helices in a helical hairpin while CetB is a peripheral membrane protein tightly associated with the membrane. CetB levels are CetA dependent. Additionally, we demonstrated that both CetA and CetB participate in complexes, including a likely CetB dimer and a complex that may include both CetA and CetB. This study provides a foundation for further characterization of signal transduction mechanisms within CetA/CetB. [source] Differentiation between electron transport sensing and proton motive force sensing by the Aer and Tsr receptors for aerotaxisMOLECULAR MICROBIOLOGY, Issue 3 2006Jessica C. Edwards Summary Aerotaxis (oxygen-seeking) behaviour in Escherichia coli is a response to changes in the electron transport system and not oxygen per se. Because changes in proton motive force (PMF) are coupled to respiratory electron transport, it is difficult to differentiate between PMF, electron transport or redox, all primary candidates for the signal sensed by the aerotaxis receptors, Aer and Tsr. We constructed electron transport mutants that produced different respiratory H+/e, stoichiometries. These strains expressed binary combinations of one NADH dehydrogenase and one quinol oxidase. We then introduced either an aer or tsr mutation into each mutant to create two sets of electron transport mutants. In vivo H+/e, ratios for strains grown in glycerol medium ranged from 1.46 ± 0.18,3.04 ± 0.47, but rates of respiration and growth were similar. The PMF jump in response to oxygen was proportional to the H+/e, ratio in each set of mutants (r2 = 0.986,0.996). The length of Tsr-mediated aerotaxis responses increased with the PMF jump (r2 = 0.988), but Aer-mediated responses did not correlate with either PMF changes (r2 = 0.297) or the rate of electron transport (r2 = 0.066). Aer-mediated responses were linked to NADH dehydrogenase I, although there was no absolute requirement. The data indicate that Tsr responds to changes in PMF, but strong Aer responses to oxygen are associated with redox changes in NADH dehydrogenase I. [source] Trypanosome Alternative Oxidase is Regulated Post-transcriptionally at the Level of RNA StabilityTHE JOURNAL OF EUKARYOTIC MICROBIOLOGY, Issue 4 2002MINU CHAUDHURI ABSTRACT In the bloodstream form of African trypanosomes, trypanosome alternative oxidase (TAO), the non-cytochrome ubiquinol:oxidoreductase, is the only terminal oxidase of the mitochondrial electron transport system. TAO is developmentally regulated during mitochondrial biogenesis in this parasite. During in vitro differentiation of Trypanosoma bmcei from the bloodstream to the procyclic form, the overall rate of oxygen consumption decreased about 80%. The mode of respiration changed over a 2- to 3-wk period from a cyanide-insensitive, SHAM-sensitive pathway to a predominantly cyanide-sensitive pathway. The TAO protein level gradually decreased to the level present in the procyclic forms during this 3-wk period. However, within the first week of differentiation, the TAO transcript level decreased about 90% and then in the following weeks it reached the level present in the established procyclic form, that is about 20% of that in bloodstream forms. Like other trypanosomatid genes TAO transcript synthesis remains unaltered in fully differentiated bloodstream and procyclic trypanosomes. The half-life of the TAO mRNA was about 3.2 h in the procyclic trypanosomes, whereas the TAO transcript level remained unaltered even after 4 h of incubation with actinomycin D in bloodstream forms. Inhibition of protein synthesis resulted in about a four-fold accumulation of the TAO transcript in the procyclic trypanosomes, comparable to the level present in the bloodstream forms. Thus, TAO is regulated at the level of mRNA stability and de novo protein synthesis is required for the reduction of the TAO mRNA pool in the procyclic form. [source] Induction of epithelial-mesenchymal transition-related genes by benzo[a]pyrene in lung cancer cellsCANCER, Issue 2 2007Ichiro Yoshino MD Abstract BACKGROUND. It is believed that epithelial-mesenchymal transition (EMT) occurs during the development and progression of cancer; however, the correlation between tobacco smoking and EMT remains to be elucidated. METHODS. Cells from the bronchioloalveolar carcinoma cell line A549 were exposed to benzo(a)pyrene (B[a]P) for 24 weeks, and morphology, proliferative activity, and gene expression profiles were analyzed. RESULTS. Although no apparent morphologic changes were observed, the B[a]P-exposed A549 cells exhibited enhanced proliferative activity in 1% bovine serum that contained medium, and dramatic changes in expression levels were observed in a large number of genes. Of those, the expression of EMT-related genes, such as migration-stimulating factor, plasminogen activator inhibitor-1, fibronectin, twist, transforming growth factor-,2, basic fibroblast growth factor, and electron transport system, were up-regulated; whereas gene expression of E-cadherin was decreased. Most enhanced expression levels remained 8 weeks after the retrieval of B[a]P in culture. CONCLUSIONS. The current results indicated that B[a]P seems to induce EMT in lung cancer cells, and it also may drive disease progression in patients with lung cancer. Cancer 2007. © 2007 American Cancer Society. [source] The relationship between cell membrane damage and lipid peroxidation under the condition of hypoxia-reoxygenation: analysis of the mechanism using antioxidants and electron transport inhibitorsCELL BIOCHEMISTRY AND FUNCTION, Issue 6 2009Daisuke Yajima Abstract We consecutively observed lipid peroxidation and cell membrane damage under the condition of hypoxia-reoxygenation (H/R) in cells and analyzed their mechanisms by using electron transport inhibitors and an antioxidant. In H/R experiments, lipid peroxidation and cell membrane damage were observed during the hypoxia phase. In the reoxygenation phase, lipid peroxidation stopped, while cell membrane damage did not. An antioxidant, n-acetylcystein (NAC), and potassium cyanide (KCN) inhibited lipid peroxidation and cell membrane damage, while rotenone did not inhibit either of them. Although antimycin A did not inhibit lipid peroxidation, it inhibited cell membrane damage during the hypoxia phase but not during the reoxygenation phase. These results suggested that lipid peroxidation can affect cell membrane damage as a trigger during the hypoxia phase and the generation of oxidative stress can vary depending on the inhibition locations in the electron transport system. Copyright © 2009 John Wiley & Sons, Ltd. [source] Azaanthraquinone inhibits respiration and in vitro growth of long slender bloodstream forms of Trypanosoma congolenseCELL BIOCHEMISTRY AND FUNCTION, Issue 3 2002Andrew Jonathan Nok Abstract An ethanolic extract of Mitracarpus scaber was found to possess in vitro and in vivo trypanocidal activity against Trypanosoma congolense. At a dosage of 50,mg kg,1 day,1 in normal saline for 5 days, the extract cured Balbc mice infected with T. congolense without any relapse. The isolated active component benz(g)isoquinoline 5,10 dione (Azaanthraquinone) (AQ) purified from the extract was found to inhibit glucose-dependent cellular respiration and glycerol-3-phosphate-dependent mitochondrial O2 assimilation of the long bloodstream forms of Trypanosoma congolense. On account of the pattern of inhibition, the target could be the mitochondrial electron transport system composed of glyceraldehyde 3-phosphate dehydrogenase (G3PDH). The azaanthraquinone specifically inhibited the reduced coenzyme Q1 -dependent O2 uptake of the mitochondria with respect to ubiquinone. The susceptible site could be due to ubiquinone redox system which links the two enzyme activities. Copyright © 2002 John Wiley & Sons, Ltd. [source] Redox Potentials of Methanophenazine and CoB-S-S-CoM, Factors Involved in Electron Transport in Methanogenic Archaea,CHEMBIOCHEM, Issue 4 2003Mario Tietze Dr. Potentially important: The redox potentials of methanophenazine and CoB-S-S-CoM (see scheme), two cofactors from methanogenic archaea, strongly support the view that methanophenazine plays a central role in the electron transport system of methane-producing archaea. These redox potentials were measured with a hanging mercury drop electrode as the working electrode and were compared to those of several phenazine ethers. [source] Redox Reactions and Electron Transfer Across the Red Cell MembraneIUBMB LIFE, Issue 7 2003Eleanor Kennett Abstract Plasma membrane electron transport systems appear to be ubiquitous. These systems are implicated in hormone signal transduction, cell growth and differentiation events as well as protection from oxidative stress. The red blood cell is constantly exposed to oxidative stress; protection against the reactive species generated during this process may be the main role of its membrane electron transport systems. Membrane redox activity has been studied for over three-quarters of a century, and yet many questions remain regarding its identity and likely roles: are electron transfers by distinct and specific mechanisms; what are the physiological donors and acceptors; and how do these systems affect metabolism? Current evidence suggests that the human erythrocyte membrane contains a number of distinct electron transfer systems, some of which, at least, involve membrane proteins, and NADH or ascorbate as electron donors. The activity of these systems appears to be closely related to the metabolic state of the cell, suggesting that mediation of reducing equivalents across the plasma membrane allows redox buffering of each environment, intra- and extracellular, by the other. We have decided to study this from a new perspective, NMR spectroscopy the area of our own technical expertise, hence this review is slanted towards this more recent analysis. IUBMB Life, 55: 375-385, 2003 [source] | ||||||||||