Steady-State Kinetics and Spectroscopic Characterization of Enzyme–tRNA Interactions for the Non-Heme Diiron tRNA-Monooxygenase, MiaE

Biochemistry ◽  
2014 ◽  
Vol 54 (2) ◽  
pp. 363-376 ◽  
Author(s):  
Bishnu P. Subedi ◽  
Andra L. Corder ◽  
Siai Zhang ◽  
Frank W. Foss ◽  
Brad S. Pierce
RSC Advances ◽  
2018 ◽  
Vol 8 (14) ◽  
pp. 7523-7532 ◽  
Author(s):  
Saba A. J. Sulaiman ◽  
Tanujjal Bora ◽  
Osama K. Abou-Zied

This work investigates the steady-state and ultrafast spectroscopy of bioconjugated gold nanoparticles and the implications on the protein binding activity and drug-loading capacity.


2009 ◽  
Vol 1794 (6) ◽  
pp. 961-967 ◽  
Author(s):  
Virendar K. Kaushik ◽  
Michael Kavana ◽  
Jessica M. Volz ◽  
Stephen C. Weldon ◽  
Susan Hanrahan ◽  
...  

2014 ◽  
Vol 19 (3) ◽  
pp. 037003 ◽  
Author(s):  
Ramu Rajasekaran ◽  
Prakasa Rao Aruna ◽  
Dornadula Koteeswaran ◽  
Ganesan Bharanidharan ◽  
Munusamy Baludavid ◽  
...  

2013 ◽  
Author(s):  
Ramu Rajasekaran ◽  
Prakasa Rao Aruna ◽  
Munusamy Balu David ◽  
Dornadula Koteeswaran ◽  
Kulandaivel Muthuvelu ◽  
...  

Biochemistry ◽  
2006 ◽  
Vol 45 (2) ◽  
pp. 552-560 ◽  
Author(s):  
Agoston Jerga ◽  
Aniruddha Raychaudhuri ◽  
Peter A. Tipton

1975 ◽  
Vol 147 (3) ◽  
pp. 513-522 ◽  
Author(s):  
P Askelöf ◽  
C Guthenberg ◽  
I Jakobson ◽  
B Mannervik

Two forms of glutathione S-aryltransferase were purified from rat liver. The only differences noted between the two forms were in the chromatographic and electrophoretic properties, which permitted the separation of the two species. The molecular weights of the enzyme and its subunits were estimated as about 50000 and 23000 respectively. The steady-state kinetics did no follow Michaelis-Menten kinetics when one substrate concentration was kept constant while the second substrate concentration was varied. Several S-substituted GSH derivatives were tested as inhibitors of the enzymic reaction. The enzyme was inactivated by thiol-group reagents.


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