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Recent developments in spin labeling

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Bioradicals Detected by ESR Spectroscopy

Part of the book series: Molecular and Cell Biology Updates ((MCBU))

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Abstract

Stable bioradical reporters can be generated by attaching a nitroxide spin label group covalently to biomolecules. The conventional electron spin resonance (ESR) spectra are sensitive to rotational motions of the spin label in the 10-11-10-8 s time regime (determined by the T2-relaxation time), and the saturation transfer ESR spectra are sensitive to molecular rotation on the 10-8-10-3 s timescale (determined by the T1-relaxation time). Applications of conventional spin label ESR include the study of lipid mobility in biological membranes, particularly of lipid-protein interactions, and of conformational changes in proteins. Applications of saturation transfer ESR (STESR) spectroscopy are confined almost exclusively to spin label studies, and include the determination of rotational diffusion rates (and hence the state of oligomeric association) of integral proteins in membranes, and of supramolecular assemblies of biomolecules.

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References

  • Altenbach, C, Marti, T, Khorana, HG, Hubbell, WL (1990) Transmembrane protein structure: Spin labeling of bacteriorhodopsin. Science 248: 1088–1092.

    Article  PubMed  CAS  Google Scholar 

  • Esmann, M, Horvath, LI, Marsh, D (1987) Saturation-transfer electron spin resonance studies on the mobility of spin labeled sodium and potassium ion activated adenosinetriphosphatase in membranes from Squalus acanthias. Biochemistry 26: 8675–8683.

    Article  PubMed  CAS  Google Scholar 

  • Esmann, M, Marsh, D (1992) Local translocational diffusion rates of membranous Na+, K+-ATPase measured by saturation transfer ESR spectroscopy. Proc. Nail. Acad. Sci. USA 89: 7606–7609.

    Article  CAS  Google Scholar 

  • Esmann, M, Hideg, K, Marsh, D (1994a) Influence of poly(ethylene glycol) and aqueous viscosity on the rotational diffusion of membranous Na, K-ATPase. Biochemistry 33: 3693–3697.

    Article  PubMed  CAS  Google Scholar 

  • Esmann, M, Karlish, SJD, Sottrup-Jensen, L, Marsh, D (1994b) Structural integrity of the membrane domains in extensively trypsinized Ma, K-ATPase from shark rectal glands. Biochemistry 33: 8044–8050.

    Article  PubMed  CAS  Google Scholar 

  • Holzenburg, A, Jones, PC, Franklin, T, Páli, T, Heimburg, T, Marsh, D, Findlay, JBC, Finbow, ME (1993) Evidence for a common structure for a class of membrane channels. Eur. J. Biochem. 213: 21–30.

    Article  PubMed  CAS  Google Scholar 

  • Horváth, LI, Brophy, PJ, Marsh, D (1990a) Influence of polar residue deletions on lipid-protein interactions with the myelin proteolipid protein. Spin label ESR studies with DM-20/lipid recombinants. Biochemistry 29: 2635–2638.

    Article  PubMed  Google Scholar 

  • Horváth, LI, Arias, HR, Hankovszky, HO, Hideg, K, Ban-antes, FJ, Marsh, D (1990b) Association of spin labeled local anaesthetics at the hydrophobic surface of acetylcholine receptor in native membranes from Torpedo marmorata. Biochemistry 29: 8707–8713.

    Article  PubMed  Google Scholar 

  • Horváth, LI, Brophy, PJ, Marsh, D (1993a) Exchange rates at the lipid-protein interface of the myelin proteolipid protein determined by saturation transfer electron spin resonance and continuous wave saturation studies. Biophys. J. 64: 622–631.

    Article  PubMed  Google Scholar 

  • Horváth, LI, Brophy, PJ, Marsh, D (1993b) Spin label saturation transfer EPR determinations of the stoichiometry and selectivity of lipid-protein interactions in the gel phase. Biochim. Biophys. Acta 1147: 277–280.

    Article  PubMed  Google Scholar 

  • Horváth, LI, Heimburg, T, Kovachev, P, Findlay, JBC, Hideg, K, Marsh, D (1995) Integration of a K+ channel-associated peptide in a lipid bilayer: Conformation, lipid-protein interactions and rotational diffusion. Biochemistry 34: 3893–3898.

    Article  PubMed  Google Scholar 

  • Hyde, JS, Swartz, HM, Antholine, WE (1979) The spin-probe-spin label method. In: L.J. Berliner (ed.): Spin Labeling. Theory and Applications. Vol. II, Academic Press, New York, pp 71–113.

    Google Scholar 

  • Khramtsov, VV, Marsh, D (1991) Measurement of the local translational diffusion rates of proteins by saturation transfer EPR spectroscopy. Biochim. Biophys. Acta 1068: 257–260.

    Article  PubMed  CAS  Google Scholar 

  • Knowles, PF, Watts, A, Marsh, D (1979) Spin label studies of lipid immobilization in dimyristoylphosphatidylcholine-substituted cytochrome oxidase. Biochemistry 18: 4480–4487.

    Article  PubMed  CAS  Google Scholar 

  • Knowles, PF, Marsh, D (1991) Magnetic resonance of membranes. Biochem. J. 214: 625–641.

    Google Scholar 

  • Likhtenstein, GI, Kulikov, AV, Kotelnikov, AI, Levchenko, LA (1986) Methods of physical labels – a combined approach to the study of microstructure and dynamics in biological systems. J. Biochem. Biophys. Methods 12: 1–28.

    Article  PubMed  CAS  Google Scholar 

  • Marsh, D (1985) ESR spin label studies of lipid-protein interactions. In: A Watts, JJHHM De Pont (eds): Progress in Protein-Lipid Interactions. Vol. 1, Elsevier, Amsterdam, pp 143–172.

    Google Scholar 

  • Marsh, D (1987) Selectivity of lipid-protein interactions. J. Bioenerg. Biomemb. 19: 677–689.

    Article  CAS  Google Scholar 

  • Marsh, D (1989) Experimental methods in spin label spectral analysis. In: LJ Berliner, J Reuben (eds): Biological Magnetic Resonance. Spin Labeling Theory and Applications. Vol. 8, Plenum, New York, pp 255–303.

    Google Scholar 

  • Marsh, D, Horváth, LI (1989) Spin label studies of the structure and dynamics of lipids and proteins in membranes. In: AJ Hoff (ed.): Advanced EPR. Applications in Biology and Biochemistry, Elsevier, Amsterdam, pp 707–752.

    Google Scholar 

  • Marsh, D (1992a) Influence of nuclear relaxation on the measurement of exchange frequencies in CW saturation EPR studies. J. Magn. Reson. 99: 332–337.

    CAS  Google Scholar 

  • Marsh, D (1992b) Exchange and dipolar spin-spin interactions and rotational diffusion in saturation transfer EPR spectroscopy. Appl. Magn. Reson. 3: 53–65.

    Article  CAS  Google Scholar 

  • Marsh, D, Horváth, LI (1992a) A simple analytical treatment of the sensitivity of saturation transfer EPR spectra to slow rotational diffusion. J. Magn. Reson. 99: 323–331.

    CAS  Google Scholar 

  • Marsh, D, Horvath, LI (1992b) Influence of Heisenberg spin exchange on conventional and phase-quadrature EPR lineshapes and intensities under saturation. J. Magn. Reson. 97: 13–26.

    CAS  Google Scholar 

  • Marsh, D (1993a) The nature of the lipid-protein interface and the influence of protein structure on protein-lipid interactions. In: A Watts (ed.): Protein-Lipid Interactions. New Comprehensive Biochemistry. Vol. 25, Elsevier, Amsterdam, pp 41–66.

    Chapter  Google Scholar 

  • Marsh, D (1993b) Progressive saturation and saturation transfer ESR for measuring exchange processes of spin labelled lipids and proteins in membranes. Chem. Soc. Rev.: 329–335.

    Google Scholar 

  • Marsh, D (1994) Spin labelling in biological systems. In: NM Atherton, MJ Davies, BC Gilbert (eds): Electron Spin Resonance, Vol. 14. Royal Society of Chemistry, Cambridge, pp 166–202.

    Chapter  Google Scholar 

  • Marsh, D (1995) Specificity of lipid-protein interactions. In: AG Lee (ed.): Biomembranes. Vol. 1, JAI Press, Greenwich, CT, pp 137–186.

    Google Scholar 

  • Páli, T, Bartucci, R, Horváth, LI, Marsh, D (1992) Distance measurements using paramagnetic ion-induced relaxation in the saturation transfer electron spin resonance of spin labeled biomolecules. Application to phospholipid bilayers and interdigitated gel phases. Biophys. J. 61: 1595–1602.

    Article  PubMed  CAS  Google Scholar 

  • Páli, T, Horváth, LI, Marsh, D (1993a) Continuous-wave saturation of two-component, inhomogeneously broadened, anisotropic EPR spectra. J. Magn. Reson. A101: 215–219.

    Google Scholar 

  • Páli, T, Bartucci, R, Horváth, LI, Marsh, D (1993b) Kinetics and dynamics of annealing during sub-gel phase formation in phospholipid bilayers. A saturation transfer electron spin resonance study. Biophys. J. 64: 1781–1788.

    Article  PubMed  Google Scholar 

  • Pates, RD, Watts, A, Uhl, R, Marsh, D (1985) Lipid-protein interactions in frog rod outer segment disc membranes. Characterization by spin labels. Biochim. Biophys. Acta 814: 389–397.

    Article  PubMed  CAS  Google Scholar 

  • Peelen, SJCJ, Sanders, JC, Hemminga, MA, Marsh, D (1992) Stoichiometry, selectivity, and exchange dynamics of lipid-protem interaction with bacteriophage Ml3 coat protein studied by spin label electron spin resonance. Effects of protein secondary structure. Biochemistry 31: 2670–2677.

    Article  PubMed  CAS  Google Scholar 

  • Ryba, NJP, Marsh, D (1992) Protein rotational diffusion and lipid/protein interactions in recombinants of bovine rhodopsin with saturated diacylphosphatidylcholines of different chain lengths studied by conventional and saturation transfer electron spin resonance. Biochemistry 31: 7511–7538.

    Article  PubMed  CAS  Google Scholar 

  • Snel, MME, Marsh, D (1993) Accessibility of spin labeled phospholipids in anionic and zwitterionic bilayer membranes to paramagnetic relaxation agents. Continuous wave power saturation EPR studies. Biochim. Biophys. Acta 1150: 155–161.

    Article  PubMed  CAS  Google Scholar 

  • Snel, MME, De Kruijff, B, Marsh, D (1993) Location of spin labelled apocytochrome c and cytochrome c relative to spin labelled lipids from spin-spin interactions in ESR saturation studies. Biophys. J. 64. A16.

    Article  Google Scholar 

  • Snel, MME, Marsh, D (1994) Membrane location of apocytochrome c and cytochrome c determined from lipid-protein spin exchange interactions by continuous wave saturation electron spin resonance. Biophys. J. 67: 737–745.

    Article  PubMed  CAS  Google Scholar 

  • Takumi, T, Ohkubo, H, Nakanishi, S (1988) Cloning of a membrane protein that induces a slow voltage-gated potassium current. Science 242: 1042–1045.

    Article  PubMed  CAS  Google Scholar 

  • Thomas, DD, Dalton, LR, Hyde, JS (1976) Rotational diffusion studied by passage saturation transfer electron paramagnetic resonance. J. Chem. Phys. 65: 3006–3024.

    Article  CAS  Google Scholar 

  • Todd, AP, Cong, J, Levinthal, F, Levinthal, C, Hubbell, WL (1989) Site-directed mutagenesis of Colicin El provides specific attachment sites for spin labels whose spectra are sensitive to local conformation. Proteins 6: 294–305.

    Article  PubMed  CAS  Google Scholar 

  • Watts, A, Volotovski, ID, Marsh, D (1979) Rhodopsin-lipid associations in bovine rod outer segment membranes. Identification of immobilized lipid by spin labels. Biochemistry. 18 5006-5013.

    Article  PubMed  CAS  Google Scholar 

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Authors and Affiliations

  1. Abteilung Spektroskopie, Max-Planck-Institut für biophysikalische Chemie, D-37077, Göttingen, Germany

    D. Marsh

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  1. D. Marsh
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Editors and Affiliations

  1. Institute for Life Support Technology of Yamagata Technopolis Foundation, 683 Kurumanomae, 990, Numagi Yamagata, Yamagata, Japan

    H. Ohya-Nishiguchi

  2. 251 Life Science Addition Membrane Bioenergetics Group, Dept. of Molecular and Cell Biology, 94720, Berkeley, CA, USA

    Lester Packer

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© 1995 Birkhäuser Verlag

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Marsh, D. (1995). Recent developments in spin labeling. In: Ohya-Nishiguchi, H., Packer, L. (eds) Bioradicals Detected by ESR Spectroscopy. MCBU Molecular and Cell Biology Updates. Birkhäuser Basel. https://doi.org/10.1007/978-3-0348-9059-5_13

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  • DOI: https://doi.org/10.1007/978-3-0348-9059-5_13

  • Publisher Name: Birkhäuser Basel

  • Print ISBN: 978-3-0348-9888-1

  • Online ISBN: 978-3-0348-9059-5

  • eBook Packages: Springer Book Archive

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