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Fourier transform infrared spectroscopy as a tool to study structural properties of cytochromes P450 (CYPs)

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Abstract

Cytochrome P450 proteins (CYPs) are a big class of heme proteins which are involved in various metabolic processes of living organisms. CYPs are the terminal catalytically active components of monooxygenase systems where the substrate binds and is hydroxylated. In order to be functionally competent, the protein structures of CYPs possess specific properties that must be explored in order to understand structure–function relationships and mechanistic aspects. Fourier transform infrared spectroscopy (FTIR) is one tool that is used to study these structural properties. The application of FTIR spectroscopy to the secondary structures of CYP proteins, protein unfolding, protein–protein interactions and the structure and dynamics of the CYP heme pocket is reviewed. A comparison with other thiolate heme proteins (nitric oxide synthase and chloroperoxidase) is also included.

The protein secondary structure, protein unfolding, redox-partner protein–protein interaction, structural changes induced by the reduction of the heme iron, and the structure and dynamics of the active site of cytochromes P450 (CYP) can be studied using Fourier transform infrared spectroscopy (FTIR). FTIR spectroscopy is a good approach for gaining a deeper insight into structure–function relationships in CYPs.

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Abbreviations

ATR:

Attenuated total reflection

CD:

Circular dichroism

CPO:

Chloroperoxidase from Caldariomyces fumago

FMN:

Flavin mononucleotide

FTIR:

Fourier transform infrared

H4B:

Tetrahydrobiopterin

HEPES:

N-(2-hydroxyethyl) piperazine-N′-(2-ethanesulfonic acid)

bsNOS:

Nitric oxide synthase from Bacillus subtilis

eNOS:

Endothelial nitric oxide synthase

iNOSox:

Oxygenase domain of inducible nitric oxide synthase

nNOSox:

Oxygenase domain of neuronal nitric oxide synthase

saNOS:

Nitric oxide synthase from Staphylococcus aureus

NAD(P)H:

Nicotinamide adenine (di)nucleotide phosphate, reduced form

NMR:

Nuclear magnetic resonance

P450:

Cytochrome P450

P450cam:

P450 from Pseudomonas putida (CYP101)

P450BMP:

The heme protein domain of P450BM-3 from Bacillus megaterium, (CYP102)

P450scc:

Cholesterol side chain cleavage P450 (CYP11A1)

P450lm2:

Microsomal P450 from rabbit (CYP2B4)

P450lm4:

Microsomal P450

P420:

Inactive form of P450

Pdx:

Putidaredoxin

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Acknowledgment

The FTIR studies were performed in the laboratory of the author at the Max Delbrück Center for Molecular Medicine at Berlin, Germany. The author thanks all former coworkers and students, in particular G. Sklenar, H. Schulze, C. Mouro, J. Contzen, N. Legrand, E. Deprez, E. Dehapiot, R. Schwarzer, A. Kariakin, M. Richter, M. Gerhardt and I. Czolkos, for contributing to projects related to the subject of this review. The author is also grateful to the collaborators G. Hui Bon Hoa and D. Davydov for helpful discussions. E. Bobrovnikova and G. Lepesheva are acknowledged for their contributions to FTIR studies on CYP2B4 and CYP11A1. The author thanks H. Frauenfelder and his students for support during the early FTIR studies on cytochromes P450 performed in the laboratory at the University of Illinois at Urbana-Champaign in 1982. Many thanks are also addressed to K. Heremans for the considerable advice given when setting up high-pressure FTIR. The German Research Foundation, the European Commission, the Institut National de la Santé et de la Recherche Médicale and the German Academic Exchange Service are acknowledged for financial support.

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  1. Max Delbrück Center for Molecular Medicine, 13125, Berlin, Germany

    Christiane Jung

  2. Medical Surface Center, KKS Ultraschall AG, 6422, Steinen, SZ, Switzerland

    Christiane Jung

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Jung, C. Fourier transform infrared spectroscopy as a tool to study structural properties of cytochromes P450 (CYPs). Anal Bioanal Chem 392, 1031–1058 (2008). https://doi.org/10.1007/s00216-008-2216-4

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