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Principal Component Analysis of Dynamical Features in the Peroxidase−Oxidase Reaction

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School of Chemical Sciences, University of Illinois at UrbanaChampaign, 600 South Mathews Avenue, Urbana, Illinois 61801
Physical Biochemistry Group, Institute for Biochemistry, Odense University, Forskerparken 10, 5230 Odense M, Denmark
Cite this: Anal. Chem. 2000, 72, 7, 1381–1388
Publication Date (Web):February 17, 2000
https://doi.org/10.1021/ac990957o
Copyright © 2000 American Chemical Society

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    Abstract

    Inherent variance due to oscillations in the peroxidase−oxidase (PO) reaction was studied using principal component analysis (PCA). The substrates were oxygen and reduced nicotinamide adenine dinucleotide (NADH). Horseradish peroxidase (HRP) catalyzed the reaction. The concentration of a cofactor, methylene blue (MB), was varied, and 2,4-dichlorophenol was kept constant. Increase in the NADH influx was used to change the reaction dynamics from periodic to chaotic. The reaction space was abstracted to the most significant, mutually independent, pairs of absorption and kinetic basis vectors (principal components). Typically, two significant principal components were extracted from the periodic time series and three from the chaotic data. The PCA models accounted for 70−97% of experimental variance. The greatest fraction of the total variance was accounted for in experiments exhibiting periodic dynamics and less than 25 nM MB. More MB induced an increased contribution of NADH to the PO oscillator variance, as did increased NADH influx. A simulated absorption time series, computed from a mass-action model of the chemistry, was analyzed by PCA as well. The comparison of simulation with experiment indicates that the chemical model renders the time series for HRP oxidation forms with fidelity, but incompletely represents NADH chemistry and other salient processes underlying the observed dynamics.

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     Current address:  Institut for Experimental Physics, Department of Biophysics, Otto von Guericke University, Universitatsplatz 2, 39106 Magdeburg, Germany.

    Cited By

    This article is cited by 11 publications.

    1. Deyana D. Lewis,, Michael L. Ruane, and, Alexander Scheeline. Biofilm Effects on the Peroxidase−Oxidase Reaction. The Journal of Physical Chemistry B 2006, 110 (15) , 8100-8104. https://doi.org/10.1021/jp0565608
    2. Cleidiane G. Zampronio,, Anastassios E. Giannakopulos,, Martin Zeller,, Eleni Bitziou,, Julie V. Macpherson, and, Peter J. Derrick. Production and Properties of Nanoelectrospray Emitters Used in Fourier Transform Ion Cyclotron Resonance Mass Spectrometry:  Implications for Determination of Association Constants for Noncovalent Complexes. Analytical Chemistry 2004, 76 (17) , 5172-5179. https://doi.org/10.1021/ac049569z
    3. Raima Larter. Understanding Complexity in Biophysical Chemistry. The Journal of Physical Chemistry B 2003, 107 (2) , 415-429. https://doi.org/10.1021/jp020856l
    4. Tatiana V. Bronnikova and, William M. Schaffer, , Lars F. Olsen. Nonlinear Dynamics of the Peroxidase−Oxidase Reaction:  I. Bistability and Bursting Oscillations at Low Enzyme Concentrations. The Journal of Physical Chemistry B 2001, 105 (1) , 310-321. https://doi.org/10.1021/jp003108+
    5. W. M. Schaffer, T. V. Bronnikova. Peroxidase-ROS interactions. Nonlinear Dynamics 2012, 68 (3) , 413-430. https://doi.org/10.1007/s11071-011-0314-x
    6. Federico I. Rosell, Hsin H. Kuo, A. Grant Mauk. NADH Oxidase Activity of Indoleamine 2,3-Dioxygenase. Journal of Biological Chemistry 2011, 286 (33) , 29273-29283. https://doi.org/10.1074/jbc.M111.262139
    7. Jeffrey A. Cramer, Karl S. Booksh. Chaos theory in chemistry and chemometrics: a review. Journal of Chemometrics 2006, 20 (11-12) , 447-454. https://doi.org/10.1002/cem.1003
    8. Jin Zhang, Ying Tang, Jia-Qing Xie, Jian-Zhang Li, Wei Zeng, Chang-Wei Hu. Study on phenol oxidation with H2O2. Journal of the Serbian Chemical Society 2005, 70 (10) , 1137-1146. https://doi.org/10.2298/JSC0510137Z
    9. Ulrich Lüttge, M.-Th. Hütt. High Frequency or Ultradian Rhythms in Plants. 2004, 235-263. https://doi.org/10.1007/978-3-642-18819-0_10
    10. Kirsten Rosendal Valeur, Robert degli Agosti. Simulations of temperature sensitivity of the peroxidase–oxidase oscillator. Biophysical Chemistry 2002, 99 (3) , 259-270. https://doi.org/10.1016/S0301-4622(02)00226-0
    11. Ewa S. Kirkor, Alexander Scheeline. Nicotinamide adenine dinucleotide species in the horseradish peroxidase–oxidase oscillator. European Journal of Biochemistry 2000, 267 (16) , 5014-5022. https://doi.org/10.1046/j.1432-1327.2000.01554.x

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