Identity of the axial ligand of the high-spin heme in cytochrome oxidase: Spectroscopic characterization of mutants in the bo-type oxidase of Escherichia coli and the aa3-type oxidase of Rhodobacter sphaeroides

Biochemistry ◽  
1993 ◽  
Vol 32 (40) ◽  
pp. 10905-10911 ◽  
Author(s):  
Melissa W. Calhoun ◽  
Jeffrey W. Thomas ◽  
John J. Hill ◽  
Jonathan P. Hosler ◽  
James P. Shapleigh ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Cytochrome Oxidase ◽  
High Spin ◽  
Rhodobacter Sphaeroides ◽  
Spectroscopic Characterization ◽  
Axial Ligand

Spectroscopic characterization of mutants supports the assignment of histidine-419 as the axial ligand of heme o in the binuclear center of the cytochrome bo ubiquinol oxidase from Escherichia coli

Biochemistry ◽  
1993 ◽  
Vol 32 (48) ◽  
pp. 13254-13261 ◽  
Author(s):  
Melissa W. Calhoun ◽  
Laura J. Lemieux ◽  
Jeffrey W. Thomas ◽  
John J. Hill ◽  
Visala Chepuri Goswitz ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Spectroscopic Characterization ◽  
Axial Ligand ◽  
Cytochrome Bo ◽  
Ubiquinol Oxidase ◽  
Binuclear Center

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.

Synthetic, Structural, and Spectroscopic Characterization of a Novel Family of High-Spin Iron(II) [(β-Diketiminate)(phosphanylphosphido)] Complexes

2017 ◽  
Vol 56 (18) ◽  
pp. 11030-11042 ◽  
Author(s):  
Rafał Grubba ◽  
Kinga Kaniewska ◽  
Łukasz Ponikiewski ◽  
Beata Cristóvão ◽  
Wiesława Ferenc ◽  
...  
Keyword(s):  
High Spin ◽  
Spectroscopic Characterization ◽  
High Spin Iron

scholarly journals Synthesis and Spectroscopic Characterization of High-Spin Mononuclear Iron(II) p-Semiquinonate Complexes

2014 ◽  
Vol 53 (23) ◽  
pp. 12240-12242 ◽  
Author(s):  
Amanda E. Baum ◽  
Heaweon Park ◽  
Sergey V. Lindeman ◽  
Adam T. Fiedler
Keyword(s):  
High Spin ◽  
Spectroscopic Characterization ◽  
Mononuclear Iron

scholarly journals Synthesis and Spectroscopic Characterization of Some New Axially Ligated Indium(III) Macrocyclic Complexes and Their Biological Activities

2014 ◽  
Vol 2014 ◽  
pp. 1-7
Author(s):  
Gauri D. Bajju ◽  
Altaf Ahmed ◽  
Deepmala Gupta ◽  
Ashu Kapahi ◽  
Gita Devi
Keyword(s):  
Biological Activities ◽  
Spectroscopic Characterization ◽  
Axial Ligand ◽  
Free Base ◽  
H Nmr ◽  
Pyramidal Geometry ◽  
The Stability ◽  
Square Pyramidal Geometry ◽  
C Nmr

The synthesis and spectroscopic characterization of new axially ligated indium(III) porphyrin complexes were reported. Chloroindium(III) porphyrin (TPPIn-Cl) was obtained in good yield by treating the corresponding free base with indium trichloride. The action of the different phenols on chloroderivatives (TPPIn-Cl) led to the corresponding phenolato complexes (TPPIn-X). These derivatives were characterized on the basis of mass spectrometry,1H-NMR, IR, and UV-visible data. The separation and isolation of these derivatives have been achieved through chromatography. The spectral properties of free base porphyrin and its corresponding metallated and axially ligated indium(III) porphyrin compounds were compared with each other. A detailed analysis of UV-Vis,1H-NMR, and IR suggested the transformation from free base porphyrin to indium(III) porphyrin. Besides,13C-NMR and fluorescence spectra were also reported and interpreted. The stability of these derivatives has also been studied through thermogravimetry. The complexes were also screened for anticancerous activities. Among all the complexes, 4-MePhO-InTPP shows highest anticancerous activity. The title complexe, TPPIn-X (where X = different phenolates), represents a five-coordinate indium(III) porphyrin complex in a square-pyramidal geometry with the phenolate anion as the axial ligand.

Overexpression and Characterization of the Rhodobacter sphaeroides PufX Membrane Protein in Escherichia coli

2006 ◽  
Author(s):  
Shiho Onodera ◽  
Hiroaki Suzuki ◽  
Yuichiro Shimada ◽  
Masayuki Kobayashi ◽  
Tsunenori Nozawa ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Membrane Protein ◽  
Rhodobacter Sphaeroides

Spectroscopic Characterization of Two New Reaction Center Mutants of the Photosynthetic Bacterium Rhodobacter Sphaeroides

1998 ◽  
pp. 747-750
Author(s):  
Arjo L. de Boer ◽  
Sieglinde Neerken ◽  
Hjalmar P. Permentier ◽  
Erik Vijgenboom ◽  
Peter Gast ◽  
...  
Keyword(s):  
Reaction Center ◽  
Rhodobacter Sphaeroides ◽  
Photosynthetic Bacterium ◽  
Spectroscopic Characterization
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