![[feed]](/style/images/feed-icon-14x14.png){kind=icon}
Tools
Tools
| Item Type: | Review |
|---|---|
| Title: | FTIR studies of the redox partner interaction in cytochrome P450: The Pdx-P450cam couple |
| Creators Name: | Karyakin, A., Motiejunas, T., Wade, R.C. and Jung, C. |
| Abstract: | Recently we have developed a new approach to study protein-protein interactions using Fourier transform infrared spectroscopy in combination with titration experiments and principal component analysis (FTIR-TPCA). In the present paper we review the FTIR-TPCA results obtained for the interaction between cytochrome P450 and the redox partner protein in two P450 systems, the Pseudomonas putida P450cam (CYP101) with putidaredoxin (P450cam-Pdx), and the Bacillus megaterium P450BM-3 (CYP102) heme domain with the FMN domain (P450BMP-FMND). Both P450 systems reveal similarities in the structural changes that occur upon redox partner complex formation. These involve an increase in beta- sheets and alpha-helix content, a decrease in the population of random coil /3(10)-helix structure, a redistribution of turn structures within the interacting proteins and changes in the protonation states or hydrogen-bonding of amino acid carboxylic side chains. We discuss in detail the P450cam-Pdx interaction in comparison with literature data and conclusions drawn from experiments obtained by other spectroscopic techniques. The results are also interpreted in the context of a 3D structural model of the Pdx-P450cam complex. |
| Keywords: | Infrared Spectroscopy, Protein-Protein Interaction, Salt Bridge, Principal Component Analysis, Cytochrome P450cam, Putidaredoxin |
| Source: | Biochimica et Biophysica Acta - General Subjects |
| ISSN: | 0006-3002 |
| Publisher: | Elsevier |
| Volume: | 1770 |
| Number: | 3 |
| Page Range: | 420-431 |
| Date: | March 2007 |
| Official Publication: | https://doi.org/10.1016/j.bbagen.2006.08.020 |
| PubMed: | View item in PubMed |
Repository Staff Only: item control page
