Proton transfer in cytochrome bo3 ubiquinol oxidase of Escherichia coli: Second-site mutations in subunit I that restore proton pumping in the mutant Asp135.fwdarw.Asn

Biochemistry ◽  
1995 ◽  
Vol 34 (13) ◽  
pp. 4428-4433 ◽  
Author(s):  
J. Arturo Garcia-Horsman ◽  
Anne Puustinen ◽  
Robert B. Gennis ◽  
Marten Wikstrom
Keyword(s):  
Escherichia Coli ◽  
Proton Transfer ◽  
Proton Pumping ◽  
Ubiquinol Oxidase ◽  
Cytochrome Bo3

scholarly journals The quinone-binding sites of the cytochrome bo3 ubiquinol oxidase from Escherichia coli

2010 ◽  
Vol 1797 (12) ◽  
pp. 1924-1932 ◽  
Author(s):  
Lai Lai Yap ◽  
Myat T. Lin ◽  
Hanlin Ouyang ◽  
Rimma I. Samoilova ◽  
Sergei A. Dikanov ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Binding Sites ◽  
Ubiquinol Oxidase ◽  
Quinone Binding ◽  
Cytochrome Bo3

Site-Directed Mutagenesis of Residues within Helix VI in Subunit I of the Cytochrome bo3 Ubiquinol Oxidase from Escherichia coli Suggests That Tyrosine 288 May Be a CuB Ligand

Biochemistry ◽  
1994 ◽  
Vol 33 (44) ◽  
pp. 13013-13021 ◽  
Author(s):  
Jeffrey W. Thomas ◽  
Melissa W. Calhoun ◽  
Laura J. Lemieux ◽  
Anne Puustinen ◽  
Marten Wikstrom ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Ubiquinol Oxidase ◽  
Cytochrome Bo3

Substitution of asparagine for aspartate-135 in subunit I of the cytochrome bo ubiquinol oxidase of Escherichia coli eliminates proton-pumping activity

Biochemistry ◽  
1993 ◽  
Vol 32 (40) ◽  
pp. 10923-10928 ◽  
Author(s):  
Jeffrey W. Thomas ◽  
Anne Puustinen ◽  
James O. Alben ◽  
Robert B. Gennis ◽  
Marten Wikstrom
Keyword(s):  
Escherichia Coli ◽  
Proton Pumping ◽  
Cytochrome Bo ◽  
Ubiquinol Oxidase ◽  
Pumping Activity

scholarly journals Identification of the ubiquinol-binding site in the cytochrome bo3-ubiquinol oxidase of Escherichia coli.

1994 ◽  
Vol 269 (46) ◽  
pp. 28834-28838
Author(s):  
R Welter ◽  
L.Q. Gu ◽  
L Yu ◽  
C.A. Yu ◽  
J Rumbley ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Binding Site ◽  
Ubiquinol Oxidase ◽  
Cytochrome Bo3

scholarly journals Fusion protein approach to improve the crystal quality of cytochrome bo3 ubiquinol oxidase from Escherichia coli

2000 ◽  
Vol 1459 (2-3) ◽  
pp. 449-455 ◽  
Author(s):  
Bernadette Byrne ◽  
Jeff Abramson ◽  
Magnus Jansson ◽  
Erik Holmgren ◽  
So Iwata
Keyword(s):  
Escherichia Coli ◽  
Fusion Protein ◽  
Crystal Quality ◽  
Ubiquinol Oxidase ◽  
Cytochrome Bo3

scholarly journals Functional expression of the eukaryotic proton pump rhodopsin OmR2 in Escherichia coli and its photochemical characterization

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Masuzu Kikuchi ◽  
Keiichi Kojima ◽  
Shin Nakao ◽  
Susumu Yoshizawa ◽  
Shiho Kawanishi ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Proton Pump ◽  
Expression System ◽  
Spectroscopic Characterization ◽  
Functional Expression ◽  
Proton Pumping ◽  
E Coli ◽  
Oxyrrhis Marina ◽  
Domains Of Life

AbstractMicrobial rhodopsins are photoswitchable seven-transmembrane proteins that are widely distributed in three domains of life, archaea, bacteria and eukarya. Rhodopsins allow the transport of protons outwardly across the membrane and are indispensable for light-energy conversion in microorganisms. Archaeal and bacterial proton pump rhodopsins have been characterized using an Escherichia coli expression system because that enables the rapid production of large amounts of recombinant proteins, whereas no success has been reported for eukaryotic rhodopsins. Here, we report a phylogenetically distinct eukaryotic rhodopsin from the dinoflagellate Oxyrrhis marina (O. marina rhodopsin-2, OmR2) that can be expressed in E. coli cells. E. coli cells harboring the OmR2 gene showed an outward proton-pumping activity, indicating its functional expression. Spectroscopic characterization of the purified OmR2 protein revealed several features as follows: (1) an absorption maximum at 533 nm with all-trans retinal chromophore, (2) the possession of the deprotonated counterion (pKa = 3.0) of the protonated Schiff base and (3) a rapid photocycle through several distinct photointermediates. Those features are similar to those of known eukaryotic proton pump rhodopsins. Our successful characterization of OmR2 expressed in E. coli cells could build a basis for understanding and utilizing eukaryotic rhodopsins.

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.

Kinetics and Intermediates of the Reaction of Fully Reduced Escherichia coli bo3 Ubiquinol Oxidase with O2

Biochemistry ◽  
2014 ◽  
Vol 53 (33) ◽  
pp. 5393-5404 ◽  
Author(s):  
Istvan Szundi ◽  
Clive Kittredge ◽  
Sylvia K. Choi ◽  
William McDonald ◽  
Jayashree Ray ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Ubiquinol Oxidase
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