scholarly journals Cardiolipin enhances the enzymatic activity of cytochrome bd and cytochrome bo3 solubilized in dodecyl-maltoside

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Amer H. Asseri ◽  
Albert Godoy-Hernandez ◽  
Hojjat Ghasemi Goojani ◽  
Holger Lill ◽  
Junshi Sakamoto ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Oxygen Consumption ◽  
Integral Membrane Proteins ◽  
Terminal Oxidase ◽  
Geobacillus Thermodenitrificans ◽  
E Coli ◽  
Cytochrome Bd ◽  
Cytochrome Bo3 ◽  
Dodecyl Maltoside ◽  
Consumption Activity

AbstractCardiolipin (CL) is a lipid that is found in the membranes of bacteria and the inner membranes of mitochondria. CL can increase the activity of integral membrane proteins, in particular components of respiratory pathways. We here report that CL activated detergent-solubilized cytochrome bd, a terminal oxidase from Escherichia coli. CL enhanced the oxygen consumption activity ~ twofold and decreased the apparent KM value for ubiquinol-1 as substrate from 95 µM to 35 µM. Activation by CL was also observed for cytochrome bd from two Gram-positive species, Geobacillus thermodenitrificans and Corynebacterium glutamicum, and for cytochrome bo3 from E. coli. Taken together, CL can enhance the activity of detergent-solubilized cytochrome bd and cytochrome bo3.

scholarly journals In Escherichia coli Ammonia Inhibits Cytochrome bo3 But Activates Cytochrome bd-I

Antioxidants ◽  
2020 ◽  
Vol 10 (1) ◽  
pp. 13
Author(s):  
Elena Forte ◽  
Sergey A. Siletsky ◽  
Vitaliy B. Borisov
Keyword(s):  
Escherichia Coli ◽  
Molecular Mechanisms ◽  
Dissociation Constants ◽  
Reductase Activity ◽  
Ammonia Concentration ◽  
High Concentration ◽  
E Coli ◽  
Cytochrome Bd ◽  
Cytochrome Bo3 ◽  
Oxygen Reductase

Interaction of two redox enzymes of Escherichia coli, cytochrome bo3 and cytochrome bd-I, with ammonium sulfate/ammonia at pH 7.0 and 8.3 was studied using high-resolution respirometry and absorption spectroscopy. At pH 7.0, the oxygen reductase activity of none of the enzymes is affected by the ligand. At pH 8.3, cytochrome bo3 is inhibited by the ligand, with 40% maximum inhibition at 100 mM (NH4)2SO4. In contrast, the activity of cytochrome bd-I at pH 8.3 increases with increasing the ligand concentration, the largest increase (140%) is observed at 100 mM (NH4)2SO4. In both cases, the effector molecule is apparently not NH4+ but NH3. The ligand induces changes in absorption spectra of both oxidized cytochromes at pH 8.3. The magnitude of these changes increases as ammonia concentration is increased, yielding apparent dissociation constants Kdapp of 24.3 ± 2.7 mM (NH4)2SO4 (4.9 ± 0.5 mM NH3) for the Soret region in cytochrome bo3, and 35.9 ± 7.1 and 24.6 ± 12.4 mM (NH4)2SO4 (7.2 ± 1.4 and 4.9 ± 2.5 mM NH3) for the Soret and visible regions, respectively, in cytochrome bd-I. Consistently, addition of (NH4)2SO4 to cells of the E. coli mutant containing cytochrome bd-I as the only terminal oxidase at pH 8.3 accelerates the O2 consumption rate, the highest one (140%) being at 27 mM (NH4)2SO4. We discuss possible molecular mechanisms and physiological significance of modulation of the enzymatic activities by ammonia present at high concentration in the intestines, a niche occupied by E. coli.

Are Escherichia coli OXPHOS complexes concentrated in specialized zones within the plasma membrane?

2008 ◽  
Vol 36 (5) ◽  
pp. 1032-1036 ◽  
Author(s):  
Tchern Lenn ◽  
Mark C. Leake ◽  
Conrad W. Mullineaux
Keyword(s):  
Escherichia Coli ◽  
Plasma Membrane ◽  
Respiratory Function ◽  
Mitochondrial Membrane ◽  
Terminal Oxidase ◽  
Inner Mitochondrial Membrane ◽  
High Concentration ◽  
E Coli ◽  
Cytochrome Bd ◽  
Biochemical Level

Most organisms are able to synthesize ATP by OXPHOS (oxidative phosphorylation). Mitochondria in eukaryotes perform OXPHOS in the inner mitochondrial membrane, whereas the plasma membrane is used by prokaryotes. However, whereas OXPHOS is a well-understood process at the biochemical level, relatively little is known about its operation at the level of the whole-organelle/cell. We observed that a fluorescently labelled terminal oxidase, the cytochrome bd complex, is heterogeneously distributed in the Escherichia coli plasma membrane. This observation forms the basis of a working hypothesis that patches of the E. coli plasma membrane (‘respirazones’) are dedicated to respiratory function by the high concentration of OXPHOS components in these zones relative to the adjacent membrane. The formulation and physiological significance of this hypothesis are discussed in this paper.

scholarly journals A factor produced by Escherichia coli K-12 inhibits the growth of E. coli mutants defective in the cytochrome bd quinol oxidase complex: enterochelin rediscovered

Microbiology ◽  
1998 ◽  
Vol 144 (12) ◽  
pp. 3297-3308 ◽  
Author(s):  
G. M. Cook ◽  
C. Loder ◽  
B. Soballe ◽  
G. P. Stafford ◽  
J. Membrillo-Hernandez ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Quinol Oxidase ◽  
E Coli ◽  
Cytochrome Bd ◽  
K 12

Cytochrome aa3 in facultatively aerobic and hyperthermophilic archaeon Pyrobaculum oguniense

2005 ◽  
Vol 51 (8) ◽  
pp. 621-627 ◽  
Author(s):  
Takuro Nunoura ◽  
Yoshihiko Sako ◽  
Takayoshi Wakagi ◽  
Aritsune Uchida
Keyword(s):  
Oxygen Consumption ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Gene Product ◽  
Respiratory Chain ◽  
Oxidase Activity ◽  
Terminal Oxidase ◽  
Hyperthermophilic Archaeon ◽  
Consumption Activity ◽  
Copper Oxidase

We partially purified and characterized the cytochrome aa3 from the facultatively aerobic and hyperthermophilic archaeon Pyrobaculum oguniense. This cytochrome aa3 showed oxygen consumption activity with N, N, N′, N′-tetramethyl-1,4-phenylenediamine and ascorbate as substrates, and also displayed bovine cytochrome c oxidase activity. These enzymatic activities of cytochrome aa3 were inhibited by cyanide and azide. This cytochrome contained heme As, but not typical heme A. An analysis of trypsin-digested fragments indicated that 1 subunit of this cytochrome was identical to the gene product of subunit I of the SoxM-type heme – copper oxidase (poxC). This is the first report of a terminal oxidase in hyperthermophilic crenarchaeon belonging to the order Thermoproteales.Key words: aerobic respiratory chain, terminal oxidase, Archaea, hyperthermophile, Pyrobaculum.

scholarly journals Homologous bd oxidases share the same architecture but differ in mechanism

2019 ◽  
Vol 10 (1) ◽  
Author(s):  
Alexander Theßeling ◽  
Tim Rasmussen ◽  
Sabrina Burschel ◽  
Daniel Wohlwend ◽  
Jan Kägi ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Escherichia Coli ◽  
Specific Inhibitor ◽  
Protonmotive Force ◽  
Geobacillus Thermodenitrificans ◽  
E Coli ◽  
Cryo Electron Microscopy ◽  
Respiratory Chains

Abstract Cytochrome bd oxidases are terminal reductases of bacterial and archaeal respiratory chains. The enzyme couples the oxidation of ubiquinol or menaquinol with the reduction of dioxygen to water, thus contributing to the generation of the protonmotive force. Here, we determine the structure of the Escherichia coli bd oxidase treated with the specific inhibitor aurachin by cryo-electron microscopy (cryo-EM). The major subunits CydA and CydB are related by a pseudo two fold symmetry. The heme b and d cofactors are found in CydA, while ubiquinone-8 is bound at the homologous positions in CydB to stabilize its structure. The architecture of the E. coli enzyme is highly similar to that of Geobacillus thermodenitrificans, however, the positions of heme b595 and d are interchanged, and a common oxygen channel is blocked by a fourth subunit and substituted by a more narrow, alternative channel. Thus, with the same overall fold, the homologous enzymes exhibit a different mechanism.

scholarly journals Characterization of cytochrome bo3 activity in a native-like surface-tethered membrane

2008 ◽  
Vol 417 (2) ◽  
pp. 555-560 ◽  
Author(s):  
Sophie A. Weiss ◽  
Richard J. Bushby ◽  
Stephen D. Evans ◽  
Peter J. F. Henderson ◽  
Lars J. C. Jeuken
Keyword(s):  
Self Assembly ◽  
Membrane System ◽  
Terminal Oxidase ◽  
E Coli ◽  
Cytochrome Bo3 ◽  
Substrate Analogues ◽  
Long Chain ◽  
Good Agreement ◽  
Tethered Membranes

We have developed a simple native-like surface-tethered membrane system to investigate the activity of cbo3 (cytochrome bo3), a terminal oxidase in Escherichia coli. The tethered membranes consist of E. coli inner-membrane extracts mixed with additional E. coli lipids containing various amounts of the cbo3 substrate UQ-10 (ubiquinol-10). Tethered membranes are formed by self-assembly from vesicles on to gold electrodes functionalized with cholesterol derivatives. cbo3 activity was monitored using CV (cyclic voltammetry) with electron transfer to cbo3 mediated by UQ-10. The apparent Km for oxygen with this system is 1.1±0.4 μM, in good agreement with values reported in the literature for whole-cell experiments and for purified cbo3. Increasing the concentration of lipophilic UQ-10 in the membrane leads to an increase in cbo3 activity. The activity of cbo3 with long-chain ubiquinones appears to be different from previous reports using short-chain substrate analogues such as UQ-1 in that typical Michaelis–Menten kinetics are not observed using UQ-10. This native-like membrane model thus provides new insights into the interaction of transmembrane enzymes with hydrophobic substrates which contrasts with studies using hydrophilic UQ analogues.

scholarly journals THE EFFECTS OF SULFATHIAZOLE AND OF PROPYL CARBAMATE ON THE RATE OF OXYGEN CONSUMPTION AND GROWTH IN ESCHERICHIA COLI

1947 ◽  
Vol 30 (3) ◽  
pp. 263-278 ◽  
Author(s):  
Kenneth C. Fisher ◽  
Florence H. Armstrong
Keyword(s):  
Escherichia Coli ◽  
Oxygen Consumption ◽  
Cell Count ◽  
Optical Density ◽  
Viable Cell ◽  
E Coli ◽  
Rate Of Growth ◽  
A Value ◽  
Rate Of Oxygen Consumption ◽  
Rates Of Growth

1. The rates of growth and of oxygen consumption by cells of E. coli have been measured under identical conditions, and the effects of sulfathiazole (ST) and of n-propyl carbamate (PC) on these two processes have been compared. 2. The rate of growth was measured by (a) the increase in the viable cell count, (b) the increase in the optical density of the culture, (c) the increase in the rate of oxygen consumption, and (d) the decrease in the ammonia of the medium. The results as indicated by these several measures were identical under the conditions of these experiments. 3. Concentrations of ST or of PC which are just sufficient to stop growth completely, lower the rate of oxygen consumption per unit of bacterial protoplasm to a value approximately 50 per cent of that seen in the absence of the inhibitor. 4. It is shown that the rate of oxygen consumption in cells from old cultures is less affected by ST than is the rate of oxygen consumption by cells from young cultures. It is probable that the rate of oxygen consumption by "old" cells is lower than that of "young" cells. 5. The effects of ST and PC on both the rate of oxygen consumption and the rate of growth are very similar, indicating in a general way, that the mechanism of the actions of these two inhibitors is similar. Furthermore, since both of them produce appreciable inhibition of the rate of oxygen consumption while they are inhibiting growth, the possibility that the effect on oxygen consumption is the immediate cause of the effect on growth must be entertained.

scholarly journals Microcin J25 Has Dual and Independent Mechanisms of Action in Escherichia coli: RNA Polymerase Inhibition and Increased Superoxide Production

2007 ◽  
Vol 189 (11) ◽  
pp. 4180-4186 ◽  
Author(s):  
Augusto Bellomio ◽  
Paula A. Vincent ◽  
Beatriz F. de Arcuri ◽  
Ricardo N. Farías ◽  
Roberto D. Morero
Keyword(s):  
Escherichia Coli ◽  
Oxygen Consumption ◽  
Rna Polymerase ◽  
Respiratory Chain ◽  
Bacterial Cells ◽  
Outer Membrane Receptor ◽  
E Coli ◽  
First Time ◽  
Intracellular Targets ◽  
Microcin J25

ABSTRACT Microcin J25 (MccJ25) uptake by Escherichia coli requires the outer membrane receptor FhuA and the inner membrane proteins TonB, ExbD, ExbB, and SbmA. MccJ25 appears to have two intracellular targets: (i) RNA polymerase (RNAP), which has been described in E. coli and Salmonella enterica serovars, and (ii) the respiratory chain, reported only in S. enterica serovars. In the current study, it is shown that the observed difference between the actions of microcin on the respiratory chain in E. coli and S. enterica is due to the relatively low microcin uptake via the chromosomally encoded FhuA. Higher expression by a plasmid-encoded FhuA allowed greater uptake of MccJ25 by E. coli strains and the consequent inhibition of oxygen consumption. The two mechanisms, inhibition of RNAP and oxygen consumption, are independent of each other. Further analysis revealed for the first time that MccJ25 stimulates the production of reactive oxygen species (O2·−) in bacterial cells, which could be the main reason for the damage produced on the membrane respiratory chain.

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