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FTIR studies of the redox partner interaction in cytochrome P450: The Pdx-P450cam couple

Item Type:Review
Title:FTIR studies of the redox partner interaction in cytochrome P450: The Pdx-P450cam couple
Creators Name:Karyakin, A. and Motiejunas, T. and 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
Page Range:420-431
Date:March 2007
Official Publication:https://doi.org/10.1016/j.bbagen.2006.08.020
PubMed:View item in PubMed

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