Title of article :
Molecular Recognition in the P450cam Monooxygenase System: Direct Monitoring of Protein–Protein Interactions by Using Optical Biosensor
Author/Authors :
Ivanov، نويسنده , , Yuri D. and Kanaeva، نويسنده , , Irina P. and Karuzina، نويسنده , , Irina I. and Archakov، نويسنده , , Alexander I. and Hoa، نويسنده , , Gaston Hui Bon and Sligar، نويسنده , , Stephen G.، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2001
Pages :
10
From page :
255
To page :
264
Abstract :
A real-time optical biosensor study on the interactions between putidaredoxin reductase (PdR), putidaredoxin (Pd), and cytochrome P450cam (P450cam) within the P450cam system was conducted. The binary Pd/P450cam and Pd/PdR complexes were revealed and kinetically characterized. The dominant role of electrostatic interactions in formation of productive electron transfer complexes was demonstrated. It was found that Pd/P450cam complex formation and decay obeys biphasic kinetics in contrast to the monophasic one for complexes formed by other redox partners within the system. Evidence for PdR/P450cam complex formation was obtained. It was found that, in contrast to Pd, which binds only to its redox partners, PdR and P450cam were able to form PdR/PdR and P450cam/P450cam complexes. A ternary PdR/Pd/P450cam complex was also registered. Its lifetime was sufficient to permit up to 60 turnovers to occur. The binding of Pd to P450cam and to PdR within the ternary complex occurred at distinct sites, with Pd serving as a bridge between the two proteins.
Keywords :
Kinetic constants , cytochrome P450cam , putidaredoxin reductase , Optical biosensor , complex formation and decay , putidaredoxin
Journal title :
Archives of Biochemistry and Biophysics
Serial Year :
2001
Journal title :
Archives of Biochemistry and Biophysics
Record number :
1618261
Link To Document :
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