Steady-State Kinetic Investigation of Cytochrome P450cam:  Interaction with Redox Partners and Reaction with Molecular Oxygen†

Biochemistry ◽  
2004 ◽  
Vol 43 (1) ◽  
pp. 271-281 ◽  
Author(s):  
Matthew M. Purdy ◽  
Laura S. Koo ◽  
Paul R. Ortiz de Montellano ◽  
Judith P. Klinman
Keyword(s):  
Steady State ◽  
Molecular Oxygen ◽  
Kinetic Investigation ◽  
Cytochrome P450cam ◽  
Redox Partners ◽  
Steady State Kinetic ◽  
State Kinetic

scholarly journals Pre-steady-state kinetic investigation of bypass of a bulky guanine lesion by human Y-family DNA polymerases

DNA Repair ◽  
2016 ◽  
Vol 46 ◽  
pp. 20-28 ◽  
Author(s):  
E. John Tokarsky ◽  
Varun V. Gadkari ◽  
Walter J. Zahurancik ◽  
Chanchal K. Malik ◽  
Ashis K. Basu ◽  
...  
Keyword(s):  
Steady State ◽  
Dna Polymerases ◽  
Kinetic Investigation ◽  
Steady State Kinetic ◽  
Y Family ◽  
State Kinetic

scholarly journals Thermodynamic and steady-state-kinetic investigation of the effect of NN′-dicyclohexylcarbodi-imide on H+ translocation by the mitochondrial cytochrome bc1 complex

1985 ◽  
Vol 225 (2) ◽  
pp. 407-411 ◽  
Author(s):  
M D Brand ◽  
M K Al-Shawi ◽  
G C Brown ◽  
B D Price
Keyword(s):  
Steady State ◽  
Thermodynamic Assessment ◽  
Cytochrome Bc1 ◽  
Kinetic Investigation ◽  
Bc1 Complex ◽  
Cytochrome Bc1 Complex ◽  
Kinetic Measurements ◽  
Steady State Kinetic ◽  
Force Ratio ◽  
State Kinetic

Steady-state kinetic measurements showed that NN′-dicyclohexylcarbodi-imide decreased the observed H+/2e ratio of H+ transport by mitochondria respiring on succinate, acting mainly at the cytochrome bc1 complex. Thermodynamic assessment of the H+/2e ratio by measuring the force ratio across the bc1 complex showed that the inhibitor did not affect H+ translocation. Possible explanations of this disagreement between methods are examined; we conclude that the inhibitor does not alter the mechanistic stoichiometry of H+ pumping by the bc1 complex.

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