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2018 | OriginalPaper | Chapter

5. Photoirradiation and Microwave Irradiation NMR Spectroscopy

Authors : Akira Naito, Yoshiteru Makino, Yugo Tasei, Izuru Kawamura

Published in: Experimental Approaches of NMR Spectroscopy

Publisher: Springer Singapore

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Abstract

In situ photoirradiation solid-state nuclear magnetic resonance (NMR) spectroscopy is designed for optical irradiation from the top part of a zirconia rotor through a glass cap, which makes it possible to efficiently irradiate the inside of the rotor. This experimental method has made it possible to observe photo-intermediates of sensory rhodopsins, such as sensory rhodopsin I (SRI) and sensory rhodopsin II (SRII), and bacteriorhodopsin (bR) Y185F mutant. In SRI, green light generates M-intermediates, which exhibit positive phototaxis, while blue light generates P-intermediates, which exhibit negative phototaxis. In SRII, green light generates M-intermediates and blue light generates O-intermediates. In Y185F-bR, O-intermediates were first observed using solid-state NMR spectroscopy. The microwave irradiation NMR spectrometer was developed in-house by modification of a commercial NMR spectrometer. A flat long copper ribbon was used as a capacitor and a half turn of copper ribbon at the edge was used as an inductor for the microwave resonance circuit, which was coaxially inserted inside the radiofrequency induction coil and allowed NMR signals to be observed under microwave irradiation conditions. The temperature of N-(4-methoxybenzylidene)-4-butylaniline (MBBA) during microwave irradiation was estimated by measuring the temperature-dependent chemical shifts, whereby different protons were found to indicate significantly different temperatures in the molecule. Liquid crystalline-isotropic phase correlation 2D NMR spectra were observed using pulsed microwave irradiation for rapid temperature jump experiments.

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Smith, S.O., de Groot, H.J.M., Gebhard, R., Courtin, J., Lugtenburg, J., Herzfeld, J., Griffin, R.G.: Structure and protein environment of the retinal chromophore in ligand- and dark-adapted bacteriorhodopsin studied by solid-state NMR. Biochemistry 28, 8897–8904 (1989)CrossRef

McDermott, A.E., Thompson, L.K., Winkel, C., Farrar, M.R., Pelletier, S., Lugtenburg, J., Herzfeld, J., Griffin, R.G.: Mechanism of proton pumping in bacteriorhodopsin by solid-state NMR: the protonation state of tyrosine in the light-adapted and M state. Biochemistry 30, 8366–8371 (1991)CrossRef

Farrar, M.R., Lakshmi, K.V., Smith, S.O., Brown, R.S., Raap, J., Lugtenburg, J., Griffin, R.G., Herzfeld, J.: Solid state NMR study of [ε-¹³C]Lys-bacteriorhodopsin: schiff base photoisomerization. Biophys. J. 65, 310–315 (1993)

Lakshmi, K.V., Farrar, M.R., Raap, J., Lugtenburg, J., Griffin, R.G., Herzfeld, J.: Solid state ¹³C and ¹⁵N NMR investigations of the N intermediate of bacteriorhodopsin. Biochemistry 33, 8853–8857 (1994)CrossRef

Feng, X., Verdegem, P.J.E., Eden, M., Sandstrom, D., Lee, Y.K., Bovee-Geurts, P.H.M., de Grip, W.J., Lugtenburg, J., de Groot, H.J.M., Levitt, M.H.: Determination of a molecular torsional angle in the metarhodopsin-I photointermediate of rhodopsin by double-quantum solid-state NMR. J. Biomol. NMR 16, 1–8 (2000)CrossRef

Crocker, E., Eilers, M., Ahuja, S., Hornak, V., Hirshfeld, A., Sheves, M., Smith, S.O.: Location of Trp265 in metarhodopsin II: implications for the activation mechanism of the visual receptor rhodopsin. J. Mol. Biol. 357, 163–172 (2006)CrossRef

Ahuja, S., Crocker, E., Eilers, M., Hornak, V., Hirshfeld, A., Ziliox, M., Syrett, N., Reeves, P.J., Khorana, H.G., Sheves, M., Smith, S.O.: Location of the retinal chromophore in the Activated state of rhodopsin. J. Biol. Chem. 284, 10190–10201 (2009)CrossRef

Hu, J.G., Sun, B.Q., Bizounok, M., Hatcher, M.E., Lansing, J.C., Raap, J., Verdegen, P.J.E., Lugtenburg, J., Griffin, R.G., Herzfeld, J.: Early and late M intermediates in the bacteriorhodopsin photocycle: a solid-state NMR study. Biochemistry 37, 8088–8096 (1998)CrossRef

Petkova, A.T., Hatanaka, M., Jaroniec, C.P., Hu, J.G., Belenky, M., Verhoeven, M., Lugtenburg, J., Griffin, R.G., Herzfeld, J.: Tryptophan interaction in bacteriorhodopsin: a heteronuclear solid-state NMR study. Biochemistry 41, 2429–2437 (2002)CrossRef

10.

Hu, J.G., Sun, B.Q., Petkova, A.T., Griffin, R.G., Herzfeld, J.: The predischarge chromophore in bacteriorhodopsin: a ¹⁵N solid-state NMR study of the L photointermediate. Biochemistry 36, 9316–9322 (1997)CrossRef

11.

Mak-Jurkauskas, M.L., Bajaj, V.S., Hornstein, M.K., Blenky, M., Griffin, R.G., Herzfeld, J.: Energy transformations early in the bacteriorhodopsin photocycle revealed by DNP-enhanced solid-state NMR. Proc. Natl. Acad. Sci. U S A 105, 883–888 (2008)CrossRef

12.

Bajaj, V.S., Mak-Jurkauskas, M.L., Belenky, M., Herzfeld, J., Griffin, R.G.: Functional and shunt state of bacteriorhodopsin resolved by 250 GHz dynamic nuclear polarization-enhanced solid-state NMR. Proc. Natl. Acad. Sci. U S A 106, 9244–9249 (2009)CrossRef

13.

Becker-Baldus, J., Bamann, C., Saxena, K., Gustmann, H., Brown, L.J., Brown, R.C.D., Reiter, C., Bamberg, E., Wachtveitl, J., Schwalbe, H., Glaubitz, C.: Enlightening the photoactive site of channelrhodopsin-2 by DNP-enhanced solid-state NMR spectroscopy. Proc. Natl. Acad. Sci. U S A 112, 9896–9901 (2015)CrossRef

14.

Kawamura, I., Kihara, N., Ohmine, M., Nishimura, K., Tuzi, S., Saitô, H., Naito, A.: Solid-state NMR studies of two backbone conformations at Tyr185 as a function of retinal configurations in the dark, light, and pressure adapted bacteriorhodopsin. J. Am. Chem. Soc. 129, 1016–1017 (2007)CrossRef

15.

Tomonaga, Y., Hidaka, T., Kawamura, I., Nishio, T., Ohsawa, K., Okitsu, T., Wada, A., Sudo, Y., Kamo, N., Ramamoorthy, A., Naito, A.: An active photoreceptor intermediate revealed by in situ photoirradiated solid-state NMR spectroscopy. Biophys. J. 101, L50–L52 (2011)CrossRef

16.

Yomoda, H., Makino, Y., Tomonaga, Y., Hidaka, T., Kawamura, I., Okitsu, T., Wada, A., Sudo, Y., Naito, A.: Color-discriminating retinal configurations of sensory rhodopsin I by photo-irradiation solid-state NMR spectroscopy. Angew. Chem. Int. Ed. 53, 6960–6964 (2014)CrossRef

17.

Naito, A., Kawamura, I.: Photoactivated structural changes in photoreceptor membrane proteins as revealed by in situ photoirradiation solid-state NMR spectroscopy. In: Separovic, F., Naito, A. (eds.) Advances in Biological Solid-State NMR: Proteins and Membrane Active Peptides, pp. 387–404. Royal Society of Chemistry, London (2014)CrossRef

18.

Naito, A., Kawamura, I., Javkhlantugs, N.: Recent solid-state NMR studies of membrane-bound peptides and proteins. Annu. Rep. NMR Spectrosc. 86, 333–411 (2015)CrossRef

19.

Oshima, K., Shigeta, A., Makino, Y., Kawamura, I., Okitsu, T., Wada, A., Tuzi, S., Iwasa, T., Naito, A.: Characterization of photo-intermediates in the photo-reaction pathways of a bacteriorhodopsin Y185F mutant using in situ photo-irradiation solid-state NMR spectroscopy. Photochem. Photobiol. Sci. 14, 1694–1702 (2015)CrossRef

20.

Gedye, R., Smith, F., Westaway, K., All, H., Baldisers, L., Laberge, L., Rousell, J.: The use of microwave ovens for rapid organic synthesis. Tetrahedron Lett. 27, 279–282 (1986)CrossRef

21.

Giguere, R.J., Bray, T.L., Duncan, S.M., Majetich, G.: Application of commercial microwave ovens to organic synthesis. Tetrahedron Lett. 27, 4945–4948 (1986)CrossRef

22.

Adam, D.: Out of the kitchen. Nature 421, 571–572 (2003)CrossRef

23.

Perreux, L., Loupy, A.: Atentative rationalization of microwave effects in organic synthesis according to the reaction medium, and mechanistic considerations. Tetrahedron 57, 9199–9223 (2001)CrossRef

24.

Lidström, P., Tiemey, J., Wathey, B., Westman, J.: Microwave assisted organic synthesis. Tetrahedron 57, 9235–9283 (2001)

25.

Bogdal, D., Lukasiewicz, M., Pielichowski, J., Miciak, A., Begdarz, Sz.: Microwave-assisted oxidation of alcohols using magtrieve. Tetrahedron 59, 649–653 (2003)

26.

Kappe, G.O.: Controlled microwave heating in modern organic synthesis. Angew. Chem. Int. Ed. 43, 6250–6284 (2004)CrossRef

27.

Yoshimura, Y., Shimizu, H., Hinou, H., Nishimura, S.-I.: A novel glycosylation concept: microwave-assisted acetal-exchange type glycosylation from methyl glycosides as donors. Tetrahedron Lett. 46, 4701–4705 (2005)CrossRef

28.

Shimizu, H., Yoshimura, Y., Hinou, H., Nishimura, S.-I.: A new glycosylation method part 3: study of microwave effects at low temperatures to control reaction pathways and reduce byproducts. Tetrahedron 64, 10091–10096 (2008)

29.

Kappe, C.O., Pieber, B., Dallinger, D.: Microwave effect in organic synthesis: myth or reality. Angew. Chem. Int. Ed. 52, 1088–1094 (2013)CrossRef

30.

Hoogenboom, R., Wiesbrock, F., Huang, H., Leenen, M.A.M., Thijis, H.M.L., van Nispen, S.F.G.M., van der Loop, M., Fustin, C.-A., Jonas, A.M., Gohy, J.-F., Schubert, U.S.: Microwave-assisted cationic ring-opening polymerization of 2-oxazolines: a powerful method for the synthesis of amphiphilic triblock copolymers. Maclomolecules 39, 4719–4725 (2006)CrossRef

31.

Iwamura, T., Ashizawa, K., Sakaguchi, M.: Efficient and echo-friendly anionic polymerization of acrylamide under microwave irradiation and hydrolysis of the obtained polymers by microwave irradiation. Macromolecules 42, 5001–5006 (2009)CrossRef

32.

Kajiwara, Y., Nagai, A., Chujo, Y.: Microwave-assisted synthesis of poly(2-hydroxyethyl methacrylate)(HEMA)/Silica hybrid using in situ polymerization method. Polymer J. 41, 1080–1084 (2009)CrossRef

33.

Yamada, S., Takasu, A., Takayama, S., Kawamura, K.: Microwave-assisted solution polycondensation of L-lactic acid using a Dean-Stark apparatus for a non-thermal microwave polymerization effect induced by the electric field. Polym. Chem. 5, 5283–5288 (2014)

34.

Pramanik, B.N., Mirza, U.A., Ing, Y.H., Liu, Y.-H., Bartner, P.L., Weber, P.C., Bose, A.K.: Microwave-enhanced enzyme reaction for protein mapping by mass spectrometry: a new approach to protein digestion in minutes. Protein Sci. 11, 2676–2687 (2002)CrossRef

35.

Huang, W., Xia, Y.-M., Gao, H., Fang, T.-J., Wang, Y., Fang, Y.J.: Enzymatic esterification between n-alcohol homologs and n-caprylic acid in non-aqueous medium under microwave irradiation. Mol. Catal. 35, 115–116 (2005)

36.

Herrero, M.A., Kremsner, J.M., Kappe, C.O.: Nonthermal microwave effects revised: on the importance of internal temperature monitoring and agitation in microwave chemistry. J. Org. Chem. 73, 36–49 (2008)CrossRef

37.

Obermayer, D., Gutmann, B., Kappe, C.O.: Microwave chemistry in silicon carbide reaction vials: separating thermal from nonthermal effects. Angew. Chem. Int. Ed. 48, 8321–8324 (2009)CrossRef

38.

Tanaka, M., Sato, M.: Microwave heating of water, ice, and saline solution: molecular dynamic study. J. Chem. Phys. 126, 034509 (2007)CrossRef

39.

Kanno, M., Nakamura, K., Kanai, K., Hoki, K., Kono, H., Tanaka, M.: Theoretical verification of nonthermal microwave effects on intramolecular reactions. J. Phys. Chem. A 116, 2177–2183 (2012)CrossRef

40.

Tsukahara, Y., Higashi, A., Yamauchi, T., Nakamura, T., Yasuda, M., Baba, A., Wada, Y.: In situ observation of nonequilibrium local heating as an origin of spherical effect of microwave on chemistry. J. Phys. Chem. C 114, 8965–8970 (2010)CrossRef

41.

Tasei, Y., Yamakami, T., Kawamura, I., Fujito, T., Ushida, K., Sato, M., Naito, A.: Mechanism for microwave heating of 1-(4′-cyanophenyl)-4-propylcyclohexane characterized by in situ microwave irradiation NMR spectroscopy. J. Magn. Reson. 254, 27–34 (2015)CrossRef

42.

Tasei, Y., Tanigawa, F., Kawamura, I., Fujito, T., Sato, M., Naito, A.: The microwave heating mechanism of N-(4-methoxybenzyliden)-4-butylaniline in liquid crystalline and isotropic phases as determined using in situ microwave irradiation NMR spectroscopy. Phys. Chem. Chem. Phys. 17, 9082–9089 (2015)CrossRef

43.

Naito, A., Imanari, M., Akasaka, K.: Separation of local magnetic fields of individual protons in nematic phase by state-correlated 2D NMR spectroscopy. J. Magn. Reson. 92, 85–93 (1991)

44.

Naito, A., Imanari, M., Akasaka, K.: State-correlated two-dimensional NMR spectroscopy: separation of local dipolar fields of protons in nematic phase of 4′-methoxybenzylidene-4-acetoxyaniline. J. Chem. Phys. 105, 4502–4510 (1996)CrossRef

45.

Akasaka, K., Kimura, M., Naito, A., Kawahara, H., Imanari, M.: Local order, conformation, and interaction in nematic 4-(n-pentyloxy-4′-cyanobiphenyl and its one-to-one mixture with 1-(4′-cyanophenyl)-4-propylcyclohexane. A study by state-correlated 1H two-dimensional NMR spectroscopy. J. Phys. Chem. 99, 9523–9529 (1995)CrossRef

46.

Naito, A., Ramamoorthy, A.: Structural studies of liquid crystalline materials using a solid state NMR technique. Thermotropic Liquid Crystal: Recent Advances, pp. 85–116, Springer, Berlin (2007)

47.

Naito, A., Tasei, Y.: Separation of local fields of individual protons in nematic phase of 4′-ethoxybenzylidene-4-n-butylaniline by microwave heating 2D NMR spectroscopy. Mater. Sci. Technol. (MS&T) 2010, 2886–2894 (2010)

48.

Akasaka, K., Naito, A., Imanari, M.: Novel method for NMR spectral correlation between the native and the denatured states of a protein. Application to ribonuclease A. J. Am. Chem. Soc. 113, 4688–4689 (1991)CrossRef

49.

Spudich, J.L., Bogomolni, R.A.: Mechanism of colour discrimination by a bacterial sensory rhodopsin. Nature 312, 509–513 (1984)CrossRef

50.

Suzuki, D., Irieda, H., Honma, M., Kawagishi, I., Sudo, Y.: Phototactic and chemotactic signal transduction by transmembrane receptors and transducers in microorganisms. Sensors 10, 4010–4039 (2010)CrossRef

51.

Chen, X., Spudich, J.L.: Demonstration of 2:2 stoichiometry in the functional SRI-HtrI signaling complex in Halobacterium membrane by gene fusion analysis. Biochemistry 41, 3891–3896 (2002)CrossRef

52.

Szundi, I., Swartz, T.E., Bogomoni, R.A.: Multicolored protein conformation state in the photocycle of transducer-free sensory rhodopsin-I. Biophys. J. 80, 469–479 (2001)CrossRef

53.

Kitajima-Ihara, T., Furutani, Y., Suzuki, D., Ihara, K., Kandori, H., Honma, M., Sudo, Y.: Salinibacter sensory rhodopsin: sensory rhodopsin I-like protein from a eubacterium. J. Biol. Chem. 283, 23533–23541 (2008)CrossRef

54.

Suzuki, D., Sudo, Y., Furutani, Y., Takahashi, H., Honnma, M., Kandori, H.: Structural changes of salinibacter sensory rhodopsin I upon formation of the K and M photointermediates. Biochemistry 47, 12750–12759 (2008)

55.

Harbison, G.S., Smith, S.O., Pardoen, J.A., Mudder, P.P.J., Lugtenburg, J., Herzfeld, J., Mishien, G.S., Griffin, R.G.: Solid-state ¹³C NMR studies of retinal in bacteriorhodopsin. Biochemistry 23, 2662–2687 (1984)

56.

Sineshchekov, O.A., Sasaki, J., Philip, S.B.J., Spudich, J.L.: A Schiff base connectivity switch in sensory rhodopsin signaling. Proc. Natl. Acad. Sci. U S A 105, 16159–16164 (2008)CrossRef

57.

Spudich, J.L., Luecke, H.: Sensory rhodopsin II: functional insight from structure. Curr. Opin. Struct. Biol. 12, 540–546 (2002)CrossRef

58.

Kamo, N., Shimono, K., Iwamoto, M., Sudo, Y.: Photochemistry and photoinduced proton-transfer by pharaonis phoborhodopsin. Biochemistry (Mosc.) 66, 1277–1282 (2001)CrossRef

59.

Gordelly, V.L., Labahn, J., Moukhametzianov, R., Efremov, R., Granzin, J., Schleslnger, R., Buldt, G., Sevopol, T., Scheldlg, A.J., Klarr, J.P., Engelhart, M.: Molecular basis of transmembrane signalling by sensory rhodopsin II-transducer complex. Nature 419, 484–487 (2002)CrossRef

60.

Shimono, K., Hayashi, T., Ikehara, Y., Sudo, Y., Iwamoto, M., Kamo, N.: Importance of the broad regional interaction for spectral tuning in Natronobacterium pharaonic phoborhodopsin (sensory rhodopsin II). J. Biol. Chem. 278, 23882–23889 (2003)CrossRef

61.

Sudo, Y., Furutani, Y., Kandori, H., Spudich, J.L.: Functional importance of the interhelical hydrogen bond between Thr204 and Tyr174 of sensory rhodopsin II and its alteration during the signalling process. J. Biol. Chem. 281, 34239–34245 (2006)CrossRef

62.

Sudo, Y., Furutani, Y., Wada, A., Ito, M., Kamo, N., Kandori, H.: Steric constraint in the primary photoproduct of an archaeal rhodopsin from regiospecific perturbation of C-D stretching vibration of the retinyl chromophore. J. Am. Chem. Soc. 127, 16036–16037 (2005)CrossRef

63.

Furutani, Y., Kamada, K., Sudo, Y., Shimono, K., Kamo, N., Kandori, H.: Structural changes of the complex between pharaonic phoborhodopsin and its cognate transducer upon formation of the M photointermediate. Biochemistry 44, 2909–2915 (2005)CrossRef

64.

Wagner, A.-A., Chzhov, I., Engelhard, M., Steinhoff, H.-J.: Time-resolved detection of transient movement of helix F in spin-labelled pharaonic sensory rhodopsin II. J. Mol. Biol. 301, 881–891 (2000)CrossRef

65.

Spudih, J.I.: Variations on a molecular switch: transport and sensory signalling by archaeal rhodopsin. Mol. Mictrobiol. 28, 1051–1058 (1998)CrossRef

66.

Yoshida, H., Sudo, Y., Shimono, K., Iwamoto, M., Kamo, N.: Transient movement of helix F revealed by photo-induced inactivation by reaction of a bulky SH-regent to cysteine-introduced pharaonis phoborhodopsin (sensory rhodopsin II). Photochem. Photobiol. Sci. 3, 537–542 (2004)CrossRef

67.

Moukhametzianov, R., Klare, J.P., Efremov, R., Baeken, C., Göppner, A., Labahn, J., Engelhard, M., Büldt, G., Gordeliy, V.I.: Development of the signal in sensory rhodopsin and its transducer to the cognate transducer. Nature 440, 115–119 (2006)CrossRef

68.

Etzkom, M., Seidel, K., Li, L., Martell, S., Geyer, M., Engelhard, M., Baldus, M.: Complex formation and light activation in membrane-embedded sensory rhodopsin II as seen by solid-state NMR spectroscopy. Structure 18, 293–300 (2010)CrossRef

69.

Kawamura, I., Yoshida, H., Ikeda, Y., Yamaguchi, S., Tuzi, S., Saitô, H., Kamo, N., Naito, A.: Dynamic change of phoborhodopsin and transducer by activation: study using D75N mutant of the receptor by site-directed solid-state ¹³C NMR. Photochem. Photobiol. 84, 921–930 (2008)

70.

Roy, S., Kikukawa, T., Sharma, P., Ksmo, N.: All-optical switching in pharaonic phoborhodopsin protein molecules. IEEE Trans. Nanobiosci. 5, 178–187 (2006)CrossRef

71.

Tateishi, Y., Abe, T., Tamogami, J., Nakano, Y., Kikukawa, T., Kamo, N., Unno, M.: Spectroscopic evidence for the formation of an N intermediate during the photocycle of sensory rhodopsin II (phoborhodopsin) from Natronobacterium pharaonic. Biochemistry 50, 2135–2143 (2011)CrossRef

72.

Lanyi, J.K.: Proton transfers in the bacteriorhodopsin photocycle. Biochim. Biophys. Acta 1757, 1012–1018 (2006)CrossRef

73.

Lanyi, J.K.: Molecular mechanism of ion transport in bacteriorhodopsin: insights from crystallographic, spectroscopic, kinetic, and mutational studies. J. Phys. Chem. B 48, 11441–11448 (2000)CrossRef

74.

Morgan, J.E., Vakkasoglu, A.S., Lanyi, J.K., Lugtenburg, J., Gennis, R.B., Maeda, G.A.: Structure changes upon deprotonation of the proton release group in the bacteriorhodopsin photocycle. Biophys. J. 103, 444–452 (2012)CrossRef

75.

Nango, E., Royant, A., Kubo, M., Nakane, T., Wlckstrand, C., Kimura, T., Tanaka, T., Tono, K., Soug, C., Tanaka, R., et al.: A three-dimensional movie of structural changes in bacteriorhodopsin. Science 354, 1552–1557 (2016)CrossRef

76.

Duriach, M., Marti, T., Khorana, H.G., Rothschild, K.J.: UV-visible spectroscopy of bacteriorhodopsin mutants: substitution of Arg-82, Asp-85, Tyr-185, and Asp-212 results in abnormal light-dark adaptation. Proc. Natl. Acad. Sci. U S A 87, 9873–9877 (1990)CrossRef

77.

Sonar, S., Krebs, M.P., Khorana, H.G., Rothchild, K.J.: Static and time-resolved absorption spectroscopy of the bacteriorhodopsin mutant Tyr185 → Phe: evidence for an equilibrium between bR570 and O-like species. Biochemistry 32, 223–2271 (1993)

78.

Rath, P., Krebs, M.P., He, Y., Khorana, H.G., Rothchild, K.J.: Fourier transform raman spectroscopy of the bacteriorhodopsin mutant Tyr185 → Phe: formation of a stable O-like species during light adaptation and detection of its transient N-like photoproduct. Biochemistry 32, 2272–2281 (1993)CrossRef

79.

Richter, H.-T., Needleman, R., Lanyi, J.K.: Perturbed interaction between residues 85 and 204 in Tyr185 → Phe and Asp85 → Glu bacteriorhodopsin. Biophys. J. 71, 3392–3398 (1996)

80.

Iwasa, T., Tokunaga, F., Yoshizawa, T.: Photochemical reaction of 13-cis-bacteriorhodopsin studied by low temperature spectroscopy. Photochem. Photobiol. 33, 539–545 (1981)CrossRef

81.

Roepe, P.D., Ahl, P.L., Herzfeld, J., Lugtenburg, J., Rothchild, K.J.: Tyrosine protonation changes in bacteriorhodopsin, a Fourier transform infrared study of BR648 and its primary photoproduct. J. Biol. Chem. 263, 5110–5117 (1988)

82.

Van Greet, A.L.: Calbration of the methanol and glycol nuclear magnetic resonance thermometers with a static thermistor probe. Anal. Chem. 40, 2227–2229 (1968)CrossRef

83.

Van Greet, A.L.: Calibration of methanol nuclear magnetic resonance thermometer at low temperature. Anal. Chem. 42, 679–680 (1970)CrossRef

84.

Bielecki, A., Burum, D.P.: Temperature dependence of ²⁰⁷Pb MAS spectra of solid lead nitrate. An accurate, sensitive thermometer for variable-temperature MAS. J. Magn. Reson. A 116, 215–220 (1995)CrossRef

85.

Zuo, C.S., Metz, K.R., Sun, Y., Sherry, A.D.: NMR temperature measurements using a paramagnetic Lanthanide complex. J. Magn. Reson. 133, 53–60 (1998)CrossRef

86.

Schuff, N.: Haeberlen, 2D Correlation spectroscopy in homonuclear dipolar-coupled solids. J. Magn. Reson. 52, 267–281 (1983)

87.

Bodenhausen, G., Freeman, R., Morris, G.A., Turner, D.L.: NMR spectra of some simple spin systems studied by two-dimensional Fourier transformation of spin echoes. J. Magn. Reson. 31, 75–95 (1978)

88.

Prasad, J.S.: Orientational order parameters and conformation of nematic p-ethoxybenzyliden-p-n-butylaniline. J. Chem. Phys. 65, 941 (1976)CrossRef

Title: Photoirradiation and Microwave Irradiation NMR Spectroscopy
Authors: Akira Naito
Yoshiteru Makino
Yugo Tasei
Izuru Kawamura
Publisher: Springer Singapore
Book: Experimental Approaches of NMR Spectroscopy
Print ISBN: 978-981-10-5965-0

Electronic ISBN: 978-981-10-5966-7

Copyright Year: 2018
DOI: https://doi.org/10.1007/978-981-10-5966-7_5