Observation of dielectric universalities in albumin, cytochrome C and Shewanella oneidensis MR-1 extracellular matrix

. 2017 Nov 16 ; 7 (1) : 15731. [epub] 20171116

Jazyk angličtina Země Anglie, Velká Británie Médium electronic

Typ dokumentu časopisecké články

Perzistentní odkaz   https://www.medvik.cz/link/pmid29147016
Odkazy

PubMed 29147016
PubMed Central PMC5691187
DOI 10.1038/s41598-017-15693-y
PII: 10.1038/s41598-017-15693-y
Knihovny.cz E-zdroje

The electrodynamics of metals is well understood within the Drude conductivity model; properties of insulators and semiconductors are governed by a gap in the electronic states. But there is a great variety of disordered materials that do not fall in these categories and still respond to external field in an amazingly uniform manner. At radiofrequencies delocalized charges yield a frequency-independent conductivity σ 1(ν) whose magnitude exponentially decreases while cooling. With increasing frequency, dispersionless conductivity starts to reveal a power-law dependence σ 1(ν)∝ν s with s < 1 caused by hopping charge carriers. At low temperatures, such Universal Dielectric Response can cross over to another universal regime with nearly constant loss ε″∝σ1/ν = const. The powerful research potential based on such universalities is widely used in condensed matter physics. Here we study the broad-band (1-1012 Hz) dielectric response of Shewanella oneidensis MR-1 extracellular matrix, cytochrome C and serum albumin. Applying concepts of condensed matter physics, we identify transport mechanisms and a number of energy, time, frequency, spatial and temperature scales in these biological objects, which can provide us with deeper insight into the protein dynamics.

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Sokolov, A. V.

Dressel, M. & Gruner, G.

Mott, N. F. & Davis, E. A.

Jonscher, A. K.

Jonscher AK. The ‘universal’ dielectric response. Nature. 1977;267:673–679. doi: 10.1038/267673a0. DOI

Dyre JC. The random free-energy barrier model for ac conduction in disordered solids. J. Appl. Phys. 1988;64:2456. doi: 10.1063/1.341681. DOI

Lunkenheimer P, Loidl A. Response of disordered matter to electromagnetic fields. Phys. Rev. Lett. 2003;91:207601. doi: 10.1103/PhysRevLett.91.207601. PubMed DOI

Dyre JC, Schrøder TB. Universality of ac conduction in disordered solids. Rev. Mod. Phys. 2000;72:873–892. doi: 10.1103/RevModPhys.72.873. PubMed DOI

Sidebottom DL. Universal Approach for Scaling the ac Conductivity in Ionic Glasses. Phys. Rev. Lett. 1999;82:3653–3656. doi: 10.1103/PhysRevLett.82.3653. DOI

Murugavel S, Roling B. AC conductivity spectra of alkali tellurite glasses: composition-dependent deviations from the Summerfield scaling. Phys. Rev. Lett. 2002;89:195902. doi: 10.1103/PhysRevLett.89.195902. PubMed DOI

Dyre JC, Maass P, Roling B, Sidebottom DL. Fundamental questions relating to ion conduction in disordered solids. Reports Prog. Phys. 2009;72:46501. doi: 10.1088/0034-4885/72/4/046501. DOI

Williams, R. J. P. In

Quinlan GJ, Martin GS, Evans TW. Albumin: Biochemical properties and therapeutic potential. Hepatology. 2005;41:1211–1219. doi: 10.1002/hep.20720. PubMed DOI

Hatefi Y, Hanstein WG, Davis KA, You KS. Structure of the mitochondrial electron transport system. Ann. N. Y. Acad. Sci. 1974;227:504–20. doi: 10.1111/j.1749-6632.1974.tb14413.x. PubMed DOI

Liu J, et al. Metalloproteins containing cytochrome, iron-sulfur, or copper redox centers. Chem. Rev. 2014;114:4366–469. doi: 10.1021/cr400479b. PubMed DOI PMC

Hayashi T, Stuchebrukhov AA. Electron tunneling in respiratory complex I. Proc. Natl. Acad. Sci. USA. 2010;107:19157–62. doi: 10.1073/pnas.1009181107. PubMed DOI PMC

Santoro C, Arbizzani C, Erable B, Ieropoulos I. Microbial fuel cells: From fundamentals to applications. A review. J. Power Sources. 2017;356:225–244. doi: 10.1016/j.jpowsour.2017.03.109. PubMed DOI PMC

White, G. F. PubMed

El-Naggar MY, Gorby Ya, Xia W, Nealson KH. The molecular density of states in bacterial nanowires. Biophys. J. 2008;95:L10–L12. doi: 10.1529/biophysj.108.134411. PubMed DOI PMC

El-Naggar MY, et al. Electrical transport along bacterial nanowires from Shewanella oneidensis MR-1. Proc. Natl. Acad. Sci. USA. 2010;107:18127–31. doi: 10.1073/pnas.1004880107. PubMed DOI PMC

Gorby YA, et al. Electrically conductive bacterial nanowires produced by Shewanella oneidensis strain MR-1 and other microorganisms. Proc. Natl. Acad. Sci. USA. 2006;103:11358–63. doi: 10.1073/pnas.0604517103. PubMed DOI PMC

Leung KM, et al. Shewanella oneidensis MR-1 bacterial nanowires exhibit p-type, tunable electronic behavior. Nano Lett. 2013;13:2407–2411. doi: 10.1021/nl400237p. PubMed DOI

Subramanian, P., Pirbadian, S., El-Naggar, M. Y. & Jensen, G. J. The ultrastructure of Shewanella oneidensis MR-1 nanowires revealed by electron cryo-tomography. PubMed PMC

Pirbadian S, et al. Shewanella oneidensis MR-1 nanowires are outer membrane and periplasmic extensions of the extracellular electron transport components. Proc. Natl. Acad. Sci. 2014;111:12883–12888. doi: 10.1073/pnas.1410551111. PubMed DOI PMC

Bodemer GJ, Antholine WA, Basova LV, Saffarini D, Pacheco AA. The effect of detergents and lipids on the properties of the outer-membrane protein OmcA from Shewanella oneidensis. JBIC J. Biol. Inorg. Chem. 2010;15:749–758. doi: 10.1007/s00775-010-0643-0. PubMed DOI

Hartshorne RS, et al. Characterization of Shewanella oneidensis MtrC: a cell-surface decaheme cytochrome involved in respiratory electron transport to extracellular electron acceptors. JBIC J. Biol. Inorg. Chem. 2007;12:1083–1094. doi: 10.1007/s00775-007-0278-y. PubMed DOI

Pitts KE, et al. Characterization of the Shewanella oneidensis MR-1 Decaheme Cytochrome MtrA. J. Biol. Chem. 2003;278:27758–27765. doi: 10.1074/jbc.M302582200. PubMed DOI

Dyre JC, et al. Fundamental questions relating to ion conduction in disordered solids. Reports Prog. Phys. 2009;72:46501. doi: 10.1088/0034-4885/72/4/046501. DOI

Roling B, Martiny C, Murugavel S. Ionic conduction in glass: new information on the interrelation between the ‘Jonscher behavior’ and the ‘nearly constant-loss behavior’ from broadband conductivity spectra. Phys. Rev. Lett. 2001;87:85901. doi: 10.1103/PhysRevLett.87.085901. PubMed DOI

Sidebottom DL, Murray-Krezan CM. Distinguishing two contributions to the nearly constant loss in ion-conducting glasses. Phys. Rev. Lett. 2002;89:195901. doi: 10.1103/PhysRevLett.89.195901. PubMed DOI

Khodadadi S, Sokolov AP. Protein dynamics: from rattling in a cage to structural relaxation. Soft Matter. 2015;11:4984–98. doi: 10.1039/C5SM00636H. PubMed DOI

Capaccioli S, Thayyil MS, Ngai KL. Critical issues of current research on the dynamics leading to glass transition. J. Phys. Chem. B. 2008;112:16035–49. doi: 10.1021/jp8057433. PubMed DOI

Capaccioli S, Ngai KL, Shinyashiki N. The Johari−Goldstein β-Relaxation of Water. J. Phys. Chem. B. 2007;111:8197–8209. doi: 10.1021/jp071857m. PubMed DOI

Ngai KL, Capaccioli S, Paciaroni A. Dynamics of hydrated proteins and bio-protectants: Caged dynamics, β-relaxation, and α-relaxation. Biochim. Biophys. Acta. 2016;1861:3553–3563. doi: 10.1016/j.bbagen.2016.04.027. PubMed DOI

von Hippel AR. The dielectric relaxation spectra of water, ice, and aqueous solutions, and their interpretation. I. Critical survey of the status-quo for water. IEEE Trans. Electr. Insul. 1988;23:801–816. doi: 10.1109/14.8745. DOI

Green JL, Fan J, Angell CA. The protein-glass analogy: New insight from homopeptide comparisons. J. Phys. Chem. 1994;98:13780–13790. doi: 10.1021/j100102a052. DOI

Iben I, et al. Glassy behavior of a protein. Phys. Rev. Lett. 1989;62:1916–1919. doi: 10.1103/PhysRevLett.62.1916. PubMed DOI

Piazza F, De Los Rios P, Sanejouand Y-H. Slow energy relaxation of macromolecules and nanoclusters in solution. Phys. Rev. Lett. 2005;94:145502. doi: 10.1103/PhysRevLett.94.145502. PubMed DOI

Xie A, van der Meer AFG, Austin RH. Excited-state lifetimes of far-infrared collective modes in proteins. Phys. Rev. Lett. 2002;88:18102. doi: 10.1103/PhysRevLett.88.018102. PubMed DOI

Shintani H, Tanaka H. Universal link between the boson peak and transverse phonons in glass. Nat. Mater. 2008;7:870–7. doi: 10.1038/nmat2293. PubMed DOI

Khodadadi S, Malkovskiy A, Kisliuk A, Sokolov AP. A broad glass transition in hydrated proteins. Biochim. Biophys. Acta. 2010;1804:15–9. doi: 10.1016/j.bbapap.2009.05.006. PubMed DOI

Surovtsev NV. Evaluation of terahertz density of vibrational states from specific-heat data: Application to silica glass. Phys. Rev. E. 2001;64:61102. doi: 10.1103/PhysRevE.64.061102. PubMed DOI

Acbas G, Niessen Ka, Snell EH. & Markelz, a G. Optical measurements of long-range protein vibrations. Nat. Commun. 2014;5:3076. doi: 10.1038/ncomms4076. PubMed DOI

Perticaroli S, Nickels JD, Ehlers G, Sokolov AP. Rigidity, secondary structure, and the universality of the boson peak in proteins. Biophys. J. 2014;106:2667–74. doi: 10.1016/j.bpj.2014.05.009. PubMed DOI PMC

Richardson DJ, et al. The ‘porin-cytochrome’ model for microbe-to-mineral electron transfer. Mol. Microbiol. 2012;85:201–212. doi: 10.1111/j.1365-2958.2012.08088.x. PubMed DOI

Paciaroni A, et al. Fingerprints of Amorphous Icelike Behavior in the Vibrational Density of States of Protein Hydration Water. Phys. Rev. Lett. 2008;101:148104. doi: 10.1103/PhysRevLett.101.148104. PubMed DOI

Liu J, Konermann L. Irreversible thermal denaturation of cytochrome C studied by electrospray mass spectrometry. J. Am. Soc. Mass Spectrom. 2009;20:819–28. doi: 10.1016/j.jasms.2008.12.016. PubMed DOI

El Kadi N, et al. Unfolding and refolding of bovine serum albumin at acid pH: ultrasound and structural studies. Biophys. J. 2006;91:3397–404. doi: 10.1529/biophysj.106.088963. PubMed DOI PMC

Brahms S, Brahms J. Determination of protein secondary structure in solution by vacuum ultraviolet circular dichroism. J. Mol. Biol. 1980;138:149–78. doi: 10.1016/0022-2836(80)90282-X. PubMed DOI

Meredith, P., Tandy, K. & Mostert, A. B. In

Mostert AB, et al. Role of semiconductivity and ion transport in the electrical conduction of melanin. Proc. Natl. Acad. Sci. 2012;109:8943–8947. doi: 10.1073/pnas.1119948109. PubMed DOI PMC

Edwards, P. P., Gray, H. B., Lodge, M. T. J. & Williams, R. J. P. Electron Transfer and Electronic Conduction through an Intervening Medium. PubMed

Waleed Shinwari M, Jamal Deen M, Starikov EB, Cuniberti G. Electrical Conductance in Biological Molecules. Adv. Funct. Mater. 2010;20:1865–1883. doi: 10.1002/adfm.200902066. DOI

Amit M, et al. Hybrid Proton and Electron Transport in Peptide Fibrils. Adv. Funct. Mater. 2014;24:5873–5880. doi: 10.1002/adfm.201401111. DOI

Shah A, et al. Electron transfer in peptides. Chem. Soc. Rev. 2015;44:1015–27. doi: 10.1039/C4CS00297K. PubMed DOI

Ron I, Pecht I, Sheves M, Cahen D. Proteins as Solid-State Electronic Conductors. Acc. Chem. Res. 2010;43:945–953. doi: 10.1021/ar900161u. PubMed DOI

Logan BE, et al. Microbial fuel cells: methodology and technology. Environ. Sci. Technol. 2006;40:5181–92. doi: 10.1021/es0605016. PubMed DOI

Logan BE, et al. Microbial Fuel Cells: Methodology and Technology. Environ. Sci. Technol. 2006;40:5181–5192. doi: 10.1021/es0605016. PubMed DOI

Richardson DJ, et al. The ‘porin-cytochrome’ model for microbe-to-mineral electron transfer. Mol. Microbiol. 2012;85:201–212. doi: 10.1111/j.1365-2958.2012.08088.x. PubMed DOI

Kittel, C.

Malinovsky VK, Novikov VN, Sokolov AP, Bagryansky VA. Light scattering by fractons in polymers. Chem. Phys. Lett. 1988;143:111–114. doi: 10.1016/0009-2614(88)87021-0. DOI

Speziale S, et al. Sound Velocity and Elasticity of Tetragonal Lysozyme Crystals by Brillouin Spectroscopy. Biophys. J. 2003;85:3202–3213. doi: 10.1016/S0006-3495(03)74738-9. PubMed DOI PMC

Griesbauer J, Wixforth A, Schneider MF. Wave Propagation in Lipid Monolayers. Biophys. J. 2009;97:2710–2716. doi: 10.1016/j.bpj.2009.07.049. PubMed DOI PMC

Yoshida K, Baron AQR, Uchiyama H, Tsutsui S, Yamaguchi T. Structure and collective dynamics of hydrated anti-freeze protein type III from 180 K to 298 K by X-ray diffraction and inelastic X-ray scattering Structure and collective dynamics of hydrated anti-freeze protein type III from 180 K to 298 K by X-ray diff. J. Chem. Phys. 2016;144:134505. doi: 10.1063/1.4944987. PubMed DOI

Kurzweil-Segev Y, et al. The role of the confined water in the dynamic crossover of hydrated lysozyme powders. Phys. Chem. Chem. Phys. 2016;18:10992–10999. doi: 10.1039/C6CP01084A. PubMed DOI

Lora Huang L-C, Huan-Cheng H-C. Adsorption and Immobilization of Cytochrome c on Nanodiamonds. Langmuir. 2004;20:5879–5884. doi: 10.1021/la0495736. PubMed DOI

Wright AK, Thompson MR. Hydrodynamic structure of bovine serum albumin determined by transient electric birefringence. Biophys. J. 1975;15:137–41. doi: 10.1016/S0006-3495(75)85797-3. PubMed DOI PMC

Koppenol WH, Rush JD, Mills JD, Margoliash E. The dipole moment of cytochrome c. Mol. Biol. Evol. 1991;8:545–58. PubMed

Masuelli MA, Masuelli MA. Study of Bovine Serum Albumin Solubility in Aqueous Solutions by Intrinsic Viscosity Measurements. Adv. Phys. Chem. 2013;2013:1–8. doi: 10.1155/2013/360239. DOI

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. 2019 Jan 25 ; 9 (7) : 3857-3867. [epub] 20190129

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