Functional Expression and Comparative Characterization of Nine Murine Cytochromes P450 by Fluorescent Inhibition Screening

2008 ◽  
Vol 36 (7) ◽  
pp. 1322-1331 ◽  
Author(s):  
Lesley A. McLaughlin ◽  
Leslie J. Dickmann ◽  
C. Roland Wolf ◽  
Colin J. Henderson
Xenobiotica ◽  
2016 ◽  
Vol 47 (11) ◽  
pp. 951-961 ◽  
Author(s):  
Gaku Okamatsu ◽  
Kei Kawakami ◽  
Tetsuya Komatsu ◽  
Takio Kitazawa ◽  
Yasuhiro Uno ◽  
...  

2016 ◽  
Vol 2 (2) ◽  
pp. 3
Author(s):  
Muhammad Irfan-maqsood ◽  
Hojjat Naderi-Meshkin ◽  
Asieh Heirani-Tabasi ◽  
Monireh Bahrami ◽  
Mahdi Mirahmadi ◽  
...  

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Masuzu Kikuchi ◽  
Keiichi Kojima ◽  
Shin Nakao ◽  
Susumu Yoshizawa ◽  
Shiho Kawanishi ◽  
...  

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.


Cellulose ◽  
2021 ◽  
Author(s):  
Mengchen Zhao ◽  
Yuko Ono ◽  
Yuichi Noguchi ◽  
Shuji Fujisawa ◽  
Tsuguyuki Saito

Author(s):  
Martha J. Larsen ◽  
Elizabeth Ruiz Lancheros ◽  
Tracey Williams ◽  
David E. Lowery ◽  
Timothy G. Geary ◽  
...  

2010 ◽  
Vol 16 (40) ◽  
pp. 12199-12206 ◽  
Author(s):  
Thomas K. Wood ◽  
Warren E. Piers ◽  
Brian A. Keay ◽  
Masood Parvez

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