Resonance energy transfer between the active sites of rabbit muscle creatine kinase: analysis by steady-state and time-resolved fluorescence

Biochemistry ◽  
1989 ◽  
Vol 28 (11) ◽  
pp. 4894-4902 ◽  
Author(s):  
Steven H. Grossman
Keyword(s):  
Creatine Kinase ◽  
Steady State ◽  
Active Sites ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Rabbit Muscle ◽  
Time Resolved Fluorescence ◽  
Muscle Creatine Kinase ◽  
Time Resolved ◽  
Muscle Creatine

Tuning of resonance energy transfer from 4′,6-diamidino-2-phenylindole to an ultrasmall silver nanocluster across the lipid bilayer

2017 ◽  
Vol 19 (40) ◽  
pp. 27305-27312 ◽  
Author(s):  
Jamuna K. Vaishnav ◽  
Tushar Kanti Mukherjee
Keyword(s):  
Energy Transfer ◽  
Steady State ◽  
Fluorescence Spectroscopy ◽  
Lipid Bilayer ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Time Resolved Fluorescence ◽  
Time Resolved ◽  
Silver Nanocluster

Liposome mediated efficient tuning of FRET between photoexcited 4′,6-diamidino-2-phenylindole (DAPI) and an ultrasmall silver nanocluster (Ag NC) has been demonstrated using steady-state and time-resolved fluorescence spectroscopy.

Sodium barbital is a slow reversible inactivator of rabbit-muscle creatine kinase

2006 ◽  
Vol 84 (2) ◽  
pp. 142-147
Author(s):  
Feng Shi ◽  
Tong-Jin Zhao ◽  
Hua-Wei He ◽  
Jie Li ◽  
Xian-Gang Zeng ◽  
...  
Keyword(s):  
Creatine Kinase ◽  
Energy Homeostasis ◽  
Inactivation Kinetics ◽  
Rabbit Muscle ◽  
Muscle Creatine Kinase ◽  
Reversible Inactivation ◽  
Inhibition Effect ◽  
Sodium Barbital ◽  
Muscle Creatine ◽  
Detailed Kinetics

As a depressant of the central nervous system, the clinical effect of sodium barbital has been extensively studied. Here we report on sodium barbital as an inhibitor of rabbit-muscle creatine kinase (CK), which plays a significant role in energy homeostasis in the muscles. Although sodium barbital gradually inhibits the activity of CK with increased concentration, the inhibition effect can be completely reversed by dilution, indicating that the inactivation process is reversible. Detailed kinetics analysis, according to a previously presented theory, indicates that sodium barbital functions as a non complexing inhibitor, and its inhibition effect on CK is a slow reversible inactivation. In this study, a kinetic model of the substrate reaction is presented, and the microscopic rate constants for the reaction of sodium barbital with the free enzyme and the enzyme–substrate complexes are determined. Kinetic analysis reveals that sodium barbital might compete with both creatine and ATP, but mainly with creatine, to inhibit the activity of CK. The results suggest that CK might be a target for sodium barbital in vivo.Key words: creatine kinase; inactivation; kinetics; sodium barbital.

Time-Resolved Fluorescence Resonance Energy Transfer Shows that the Bacterial Multidrug ABC Half-Transporter BmrA Functions as a Homodimer†

Biochemistry ◽  
2005 ◽  
Vol 44 (11) ◽  
pp. 4312-4321 ◽  
Author(s):  
Olivier Dalmas ◽  
Marie-Ange Do Cao ◽  
Miguel R. Lugo ◽  
Frances J. Sharom ◽  
Attilio Di Pietro ◽  
...  
Keyword(s):  
Energy Transfer ◽  
Fluorescence Resonance Energy Transfer ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Time Resolved Fluorescence ◽  
Time Resolved ◽  
Fluorescence Resonance

Recommendations for the Reduction of Compound Artifacts in Time-Resolved Fluorescence Resonance Energy Transfer Assays

2007 ◽  
Vol 5 (3) ◽  
pp. 363-372 ◽  
Author(s):  
Pierre-Eloi Imbert ◽  
Vincent Unterreiner ◽  
Daniela Siebert ◽  
Hanspeter Gubler ◽  
Christian Parker ◽  
...  
Keyword(s):  
Energy Transfer ◽  
Fluorescence Resonance Energy Transfer ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Time Resolved Fluorescence ◽  
Time Resolved ◽  
Fluorescence Resonance
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