Articles | Volume 2, issue 1
https://doi.org/10.5194/mr-2-465-2021
© Author(s) 2021. This work is distributed under
the Creative Commons Attribution 4.0 License.
the Creative Commons Attribution 4.0 License.
Special issue:
https://doi.org/10.5194/mr-2-465-2021
© Author(s) 2021. This work is distributed under
the Creative Commons Attribution 4.0 License.
the Creative Commons Attribution 4.0 License.
Introduction to a special issue of Magnetic Resonance in honour of Robert Kaptein at the occasion of his 80th birthday
Bijvoet Centre for Biomolecular Research, Utrecht University, 3584 CH Utrecht, the Netherlands
Konstantin Ivanov
International Tomography Center, Siberian Branch of the Russian
Academy of Sciences, Novosibirsk 630090, Russia
Department of Natural Sciences, Novosibirsk State University,
Novosibirsk 630090, Russia
deceased, 5 March 2021
Jörg Matysik
CORRESPONDING AUTHOR
Institut für Analytische Chemie, Universität Leipzig, Linnéstraße 3, 04189 Leipzig, Germany
Related authors
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Corinna Dietrich, Julia Wissel, Oliver Lorenz, Arafat Hossain Khan, Marko Bertmer, Somayeh Khazaei, Daniel Sebastiani, and Jörg Matysik
Magn. Reson., 2, 751–763, https://doi.org/10.5194/mr-2-751-2021, https://doi.org/10.5194/mr-2-751-2021, 2021
Short summary
Short summary
Quantum-rotor-induced polarization, also called the Haupt effect, is a hyperpolarization technique in NMR relying on the coupling of nuclear spin states to rotational quantum states. The classic molecule showing this effect is γ-picoline. One might assume that many other molecules carrying a methyl group might also show this effect. Here we explore, using a heuristic approach, other molecules which appear to be promising candidates.
Geertje J. Janssen, Patrick Eschenbach, Patrick Kurle, Bela E. Bode, Johannes Neugebauer, Huub J. M. de Groot, Jörg Matysik, and Alia Alia
Magn. Reson., 1, 261–274, https://doi.org/10.5194/mr-1-261-2020, https://doi.org/10.5194/mr-1-261-2020, 2020
Short summary
Short summary
Natural photosynthetic reaction centers (RCs) are built up by two parallel branches of cofactors. While photosystem II and purple bacterial RCs selectively use one branch for light-driven electron transfer, photosystem I, as also shown here, is using both branches. Comparing NMR chemical shifts, we shown that the two donor cofactors in photosystem I are similarly distinguished to those in purple bacterial RCs (Schulten et al., 2002; Biochemistry 41, 8708). Alternative reasons are discussed.
Cited articles
Akasaka, K., Fujii, S., and Kaptein, R.: Exposure of Aromatic Residues of Streptomyces Subtilisin Inhibitor. A Photo-CIDNP study, J. Biochem.-Tokyo, 89, 1945–1949, https://doi.org/10.1093/oxfordjournals.jbchem.a133396, 1981.
Bargon, J., Fischer, H., and Johnson, U.: Kernresonanz-Emissionslinien
während rascher Radikalreaktionen. 1. Aufnahmeverfahren und Beispiele,
Z. Naturforsch., 22a, 1551–1555, https://doi.org/10.1515/zna-1967-1014, 1967.
Berliner, L. J. and Kaptein, R.: NMR Characterization of Aromatic Residues
of α-Lactalbumins. Laser Photo Chemically Induced Dynamic Nuclear
Polarization Nuclear Magnetic Resonance Studies of Surface Exposure,
Biochemistry, 20, 799–807, https://doi.org/10.1021/bi00507a023, 1981.
Bernard, C., Houben, K., Derix, N. M., Marks, D., van der Horst, M. A.,
Hellingwerf, K. J., Boelens, R., Kaptein, R., and van Nuland, N. A. J.: The
solution structure of a transient photoreceptor intermediate: Δ25
photoactive yellow protein, Structure, 13, 953–962, https://doi.org/10.1016/j.str.2005.04.017, 2005.
Boelens, R., Scheek, R. M., Dijkstra, K., and Kaptein, R.: Sequential
Assignment of Imino- and Amino-Proton Resonances in 1H NMR Spectra of
Oligonucleotides by Two-Dimensional NMR Spectroscopy. Application to a lac Operator Fragment, J. Magn. Reson., 62, 378–386,
https://doi.org/10.1016/0022-2364(85)90207-0, 1985.
Boelens, R., Scheek, R. M., van Boom, J. H., and Kaptein, R.: Complex of lac repressor Headpiece with a 14 base-pair lac operator fragment studied by two-dimensional nuclear magnetic resonance, J. Mol. Biol., 193, 213–216, https://doi.org/10.1016/0022-2836(87)90638-3, 1987.
Boelens, R., Koning, T. M. G., and Kaptein, R.: Determination of
biomolecular structures from proton-proton NOE's using a relaxation matrix
approach, J. Mol. Struct., 173, 299–311, https://doi.org/10.1016/0022-2860(88)80062-0, 1988.
Boelens, R., Koning, T. M. G., van der Marel, G. A., van Boom, J. H., and
Kaptein, R.: Iterative procedure for structure determination from
proton-proton NOE's using a full relaxation matrix approach. Application to
a DNA octamer, J. Magn. Reson., 82, 290–308,
https://doi.org/10.1016/0022-2364(89)90032-2, 1989a.
Boelens, R., Vuister, G. W., Koning, T. M. G., and Kaptein, R.: Observation
of spin-diffusion in biomolecules by three-dimensional NOE-NOE spectroscopy,
J. Am. Chem. Soc., 111, 8525–8526, https://doi.org/10.1021/ja00204a039, 1989b.
Bonvin, A. M. J. J., Vis, H., Breg, J. N., Burgering, M. J. M., Boelens, R.,
and Kaptein, R.: NMR solution structure of the Arc repressor using
relaxation matrix calculations, J. Mol. Biol., 236, 328–341,
https://doi.org/10.1006/jmbi.1994.1138, 1994.
Breg, J. N., van Opheusden, J. H. J., Burgering, M. J. M., Boelens, R., and
Kaptein, R.: The structure of Arc repressor in solution. A family of
β-sheet DNA-binding proteins, Nature, 346, 586–589, https://doi.org/10.1038/346586a0, 1990.
Brünger, A. T.: X-PLOR, Version 3.1, A System for X-ray Crystallography and NMR, Yale University Press, ISBN 978-0300054026, 1992.
Brünger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P.,
Grosse-Kunstleve, R. W., Jiang, J. S., Kuszewski, J., Nilges, M., Pannu, N.
S., Read, R. J., Rice, L. M., Simonson, T., and Warren, G. L.:
Crystallography & NMR system: A new software suite for macromolecular
structure determination, Acta Crystallogr. D, 54, 905–921,
https://doi.org/10.1107/s0907444998003254, 1998.
Buck, F., Hahn, K. D., Zemann, W., Rüterjans, H., Sadler, J. R.,
Beyreuther, K., Kaptein, R., Scheek, R., and Hull, W. E.: NMR Study of the Interaction between the lac Repressor and the lac Operator, Eur. J. Biochem., 132, 321–327, https://doi.org/10.1111/j.1432-1033.1983.tb07365.x, 1983.
Burgering, M. J. M., Boelens, R., Gilbert, D. E., Breg, J. N., Knight, K.
L., Sauer, R. T., and Kaptein, R.: Solution Structure of Dimeric Mnt
Repressor (1-76), Biochemistry, 33, 15036–15045, https://doi.org/10.1021/bi00254a012, 1994.
Canioni, P., Cozzone, P. J., and Kaptein, R.: 360 MHz Laser Photo-CIDNP of
Porcine Pancreatic Colipase A. A Study of the Aromatic Surface Residues,
FEBS Lett., 111, 219–222, https://doi.org/10.1016/0014-5793(80)80797-6, 1980.
Chuprina, V. P., Rullmann, J. A. C., Lamerichs, R. M. J. N., van Boom, J.
H., Boelens, R., and Kaptein, R.: Structure of the Complex of lac Repressor Headpiece and an 11 Base Pair Half-Operator determined by NMR Spectroscopy and Restrained Molecular Dynamics, J. Mol. Biol., 234, 446–462,
https://doi.org/10.1006/jmbi.1993.1598, 1993.
Closs, G. L. and Closs, L. E.: Induced dynamic nuclear spin polarization in
reactions of photochemically and thermally generated triplet
diphenylmethylene, J. Am. Chem. Soc., 91, 4549–4550,
doi:https://doi.org/10.1021/ja01044a041, 1969.
Craven, C. J., Derix, N. M., Hendriks, J., Boelens, R., Hellingwerf, K. J.,
and Kaptein, R.: Probing the nature of the blue-shifted intermediate of
photoactive yellow protein in solation by NMR: Hydrogen-deuterium exchange
data and pH studies, Biochemistry, 39, 14392–14399, https://doi.org/10.1021/bi001628p, 2000.
de Galan, L.: De instrumentele omwenteling: analytische chemie, in: De
geschiedenis van de scheikunde in Nederland 3. De ontwikkeling van de chemie
van 1945 tot het begin van de jaren tachtig, Delft University Press, Delft, 87–103, 2004.
Dekker, N., Cox, M., Boelens, R., Verrijzer, C. P., van der Vliet, P. C.,
and Kaptein, R.: Solution structure of the POU-specific DNA binding domain
of Oct-1, Nature, 362, 852–855, https://doi.org/10.1038/362852a0, 1993.
de Marco, A., Mayo, K. H., Bartolotti, F., Scalia, S., Menegatti, E., and
Kaptein, R.: Proton NMR and photo-CIDNP studies of peptide fragments
obtained by controlled proteolysis of mouse epidermal growth factor, J.
Biol. Chem., 261, 13510–13516, https://doi.org/10.1016/S0021-9258(18)67048-6, 1986a.
de Marco, A., Zetta, L., Petros, A. M., Llinas, M., Boelens, R., and
Kaptein, R.: Kringle 4 from human plasminogen: A proton Magnetic Resonance
study via two-dimensional photochemically induced dynamic nuclear
polarization spectroscopy, Biochemistry, 25, 7918–7923, https://doi.org/10.1021/bi00372a020, 1986b.
den Hollander, J. A. and Kaptein, R.: Radical Pair Substitution in CIDNP.
Spin-Uncorrelated Geminate Radical Pairs, Chem. Phys. Lett., 41, 257–263,
https://doi.org/10.1016/0009-2614(76)80805-6, 1976.
Drenth, W.: 120 jaar fysisch-organische chemie in Nederland 1874–1994, Utrecht, 2001.
Drenth, W. and Verhoeven, J. W.: Fysische-organische chemie: grote bloei na
een aarzelend begin, in: De geschiedenis van de scheikunde in Nederland 3.
De ontwikkeling van de chemie van 1945 tot het begin van de jaren tachtig,
Delft University Press, Delft, 243–255, 2004.
Düx, P., Rubinstenn, G., Vuister, G. W., Boelens, R., Mulder, F. A. A., Hård, K., Hoff, W. D., Kroon, A. R., Crielaard, W., Hellingwerf, K. J., and Kaptein, R.: Solution structure and backbone dynamics of the photoactive yellow protein, Biochemistry, 37, 12689–12699, https://doi.org/10.1021/bi9806652, 1998.
Egmond, M. R., Hore, P. J., and Kaptein, R.: Photo-CIDNP 1H-NMR Studies of Bovine Pancreactic Phospholipase A2 and its Zymogen, Biochim. Biophys. Acta, 744, 23–27, https://doi.org/10.1016/0167-4838(83)90335-7, 1983.
Eijkelenboom, A. P. A. M., Lutzke, R. A. P., Boelens, R., Plasterk, R. H.
A., Kaptein, R., and Hård, K.: The DNA-Binding domain of HIV-1 Iintegrase
has an SH3-like fold, Nat. Struct. Biol., 2, 807–810, https://doi.org/10.1038/nsb0995-807, 1995.
Eijkelenboom, A. P. A. M., van den Ent, F. M. I., Wechselberger, R.,
Plasterk, R. H. A., Kaptein, R., and Boelens, R.: Refined solution structure
of the dimeric N-terminal HHCC domain of HIV-2 integrase, J. Biomol. NMR,
18, 119–128, https://doi.org/10.1023/a:1008342312269, 2000.
Feeney, J., Roberts, G. C. K., Kaptein, R., Birdsall, B., Gronenborn, A.,
and Burgen, A. S. V.: Photo-CIDNP Studies of the Influence of Ligand Binding
on the Surface Accessibility of Aromatic Residues in Dihydrofolate
Reductase, Biochemistry, 19, 2466–2472, https://doi.org/10.1021/bi00552a026, 1980.
Freeman, R., Hill, H. D. W., and Kaptein, R.: Proton-Decoupled NMR Spectra
of Carbon-13 With the Nuclear Overhauser Effect Suppressed, J. Magn. Reson., 7, 327–329, https://doi.org/10.1016/0022-2364(72)90194-1, 1972.
Garner, W. H., Spector, A., Schleich, T., and Kaptein, R.: Determination of
the solvent accessibility of specific aromatic residues in gamma-crystallin
by Photo-CIDNP NMR measurements, Curr. Eye Res., 3, 127–135,
https://doi.org/10.3109/02713688408997194, 1984.
Garssen, G. J., Kaptein, R., Schoenmakers, J. G. G., and Hilbers, C. W.: A
photo-CIDNP study of the interaction of oligonucleotides with gene-5 protein
of bacteriophage M13, P. Natl. Acad. Sci. USA, 75, 5281–5285,
https://doi.org/10.1073/pnas.75.11.5281, 1978.
Griesinger, C., Sørensen, O. W., and Ernst, R. R.: A practical approach
to three-dimensional NMR spectroscopy, J. Magn. Reson., 73, 574–579, https://doi.org/10.1016/0022-2364(87)90027-8, 1987.
Härd, T., Kellenbach, E., Boelens, R., Maler, B. A., Dahlman, K.,
Freedman, L. P., Carlstedt-Duke, J., Yamamoto, K. R., Gustafsson, J. A., and
Kaptein, R.: Solution Structure of the Glucocorticoid Receptor DNA-Binding
Domain, Science, 249, 157–160, https://doi.org/10.1126/science.2115209, 1990.
Hoff, W. D., Düx, P., Hård, K., de Vreese, B., Nugteren-Roodzant, I. M.,
Crielaard, W., Boelens, R., Kaptein, R., van Beeumen, J., and Hellingwerf,
K. J.: Thiol ester-linked p-coumaric acid as a new photoactive cofactor in a
rhodopsin-like protein, Biochemistry, 33, 13959–13962, https://doi.org/10.1021/bi00251a001, 1994.
Hore, P. J. and Kaptein, R.: Photo-CIDNP of Biological Molecules using
Continuous Wave and Time-Resolved Methods, ACS Symp. Ser., 191, 285–318,
https://doi.org/10.1021/bk-1982-0191.ch015, 1982.
Hore, P. J., Zuiderweg, E. R. P., Kaptein, R., and Dijkstra, K.: Flash
Photolysis NMR. CIDNP Time Dependence in Cyclic Photochemical Reactions,
Chem. Phys. Lett., 83, 376–383, https://doi.org/10.1016/0009-2614(81)85483-8, 1981.
Hore, P. J., Volbeda, A., Dijkstra, K., and Kaptein, R.: Photo-Reduction of
Flavin by NADH – a flash-photolysis photo-CIDNP study, J. Am. Chem. Soc.,
104, 6262–6267, https://doi.org/10.1021/ja00387a017, 1982.
Hore, P. J., Stob, S., Kemmink, J., and Kaptein, R.: An Exception to the
CIDNP Sign Rules, Chem. Phys. Lett., 98, 409–413,
https://doi.org/10.1016/0009-2614(83)80077-3, 1983.
Hsu, S. T. D., Breukink, E., Tischenko, E., Lutters, M. A. G., de Kruijff,
B., Kaptein, R., Bonvin, A. M. J. J., and van Nuland, N. A. J.: The
nisin-lipid II complex reveals a pyrophosphate cage that provides a
blueprint for novel antibiotics, Nat. Struct. Mol. Biol., 11, 963–967,
https://doi.org/10.1038/nsmb830, 2004.
Ivanov, K. L., Stass, D. V., Kalneus, E. V., Kaptein, R., and Lukzen, N. N.:
Theoretical Treatment of Degenerate Electron Exchange and Dimerization in
Spin Dynamics of Radical Ion Pairs as Observed by Magnetic Field Effects,
Appl. Magn. Reson., 44, 217–232, https://doi.org/10.1007/s00723-012-0413-y, 2013.
Ivanov, K. L., Pravdivtsev, A. N., Yurkovskaya, A. V., Vieth, H. M., and
Kaptein, R.: The role of level anti-crossings in nuclear spin
hyperpolarization, Prog. Nucl Mag. Res. Sp., 81, 1–36,
https://doi.org/10.1016/j.pnmrs.2014.06.001, 2014.
Jansen, E. H. J. M., Meyer, H., de Haas, G. H., and Kaptein, R.: A
Photo-CIDNP Study of Pancreatic Phospholipase A2. NMR Assignments of some
Aromatic Residues, J. Biol. Chem., 253, 6346–6347,
https://doi.org/10.1016/S0021-9258(19)46939-1, 1978.
Jansen, E. H. J. M., van Scharrenburg, G. J. M., Slotboom, A. J., de Haas,
G. H., and Kaptein, R.: A 360 MHz Photo-CIDNP Study of Bovine Pancreatic
Phospholipase A2. Observation of a pH Dependent Conformational Change, J.
Am. Chem. Soc., 101, 7397–7399, https://doi.org/10.1021/ja00518a045, 1979.
Kalodimos, C. G., Bonvin, A. M. J. J., Salinas, R. K., Wechselberger, R.,
Boelens, R., and Kaptein, R.: Plasticity in protein-DNA recognition: lac repressor interacts with its natural operator O1 through alternative conformations of its DNA-binding domain, EMBO J., 21, 2866–2876, https://doi.org/10.1093/emboj/cdf318, 2002.
Kalodimos, C. G., Biris, N., Bonvin, A. M. J. J., Levandoski, M. M.,
Guennuegues, M., Boelens, R., and Kaptein, R.: Structure and flexibility
adaptation in nonspecific and specific protein-DNA complexes, Science, 305,
386–389, https://doi.org/10.1126/science.1097064, 2004a.
Kalodimos, C. G., Boelens, R., and Kaptein, R.: Toward an integrated model
of protein-DNA recognition as inferred from NMR studies on the Lac repressor
system, Chem. Rev., 104, 3567–3586, https://doi.org/10.1021/cr0304065, 2004b.
Kaptein, R.: Simple Rules for Chemically Induced Dynamic Nuclear
Polarization, J. Chem. Soc. Chem. Comm., 732–733, https://doi.org/10.1039/c29710000732, 1971a.
Kaptein, R.: Chemically Induced Dynamic Nuclear Polarization, PhD thesis, Leiden University, the Netherlands, 1971b.
Kaptein, R.: Chemically Induced Dynamic Nuclear Polarization. IX. Reactions
competitive with germinate recombination of radical pairs, J. Am. Chem.
Soc., 94, 6262–6269, https://doi.org/10.1021/ja00773a002, 1972a.
Kaptein, R.: Chemically Induced Dynamic Nuclear Polarization. VIII. Spin
Dynamics and Diffusion of Radical Pairs, J. Am. Chem. Soc., 94, 6251–6262,
https://doi.org/10.1021/ja00773a001, 1972b.
Kaptein, R.: Photo-CIDNP Studies of Proteins, in: Biological Magnetic
Resonance, 1st edn., edited by: Berliner, L. J. and Rueben, J., Springe US, Biological Magnetic Resonance, 4, 145–191, 1982.
Kaptein, R.: The Early Days of CIDNP, in: Encyclopedia of Magnetic Resonance, edited by: Harris, R. K. and Wasylishen, R., John Wiley, Chichester, https://doi.org/10.1002/9780470034590.emrhp0092, 2007.
Kaptein, R. and den Hollander, J. A.: Chemically Induced Dynamic Nuclear
Polarization. X. On the Magnetic Field Dependence, J. Am. Chem. Soc., 94,
6269–6280, https://doi.org/10.1021/ja00773a003, 1972.
Kaptein, R. and Oosterhoff, L. J.: Chemically induced dynamic nuclear
polarization. III. (anomalous multiplets of radical coupling and disproportionation products), Chem. Phys. Lett., 4, 214–216, https://doi.org/10.1016/0009-2614(69)80105-3, 1969a.
Kaptein, R. and Oosterhoff, L. J.: Chemically induced dynamic nuclear
polarization. II. (Relation with anomalous ESR spectra), Chem. Phys. Lett.,
4, 195–197, https://doi.org/10.1016/0009-2614(69)80098-9, 1969b.
Kaptein, R., Fráter-Schröder, M., and Oosterhoff, L. J.: Chemically
Induced Dynamic Nuclear Polarization. V. NMR Enhancements in Biradical
Products, Chem. Phys. Lett., 12, 16–19, https://doi.org/10.1016/0009-2614(71)80606-1, 1971a.
Kaptein, R., Verheus, F. W., and Oosterhoff, L. J.: Chemically Induced
Dynamic Nuclear Polarization. VI. Sign Reversal of the Polarization in the
Reaction of Isobutyryl Peroxide with Bromotrichloromethane, J. Chem. Soc. Chem. Comm., 877–878, https://doi.org/10.1039/c29710000877, 1971b.
Kaptein, R., Brokken-Zijp, J., and de Kanter, F. J. J.: Chemically Induced
Dynamic Nuclear Polarization. XI. Thermal Decomposition of Acetyl Peroxide,
J. Am. Chem. Soc., 94, 6280–6287, https://doi.org/10.1021/ja00773a004, 1972.
Kaptein, R., Freeman, R., Hill, H. D. W., and Bargon, J.: Carbon-13 CIDNP in
the Reversible Addition of Pentafluorobenzoyloxy Radicals to Chlorobenzene, J. Chem. Soc. Chem. Comm., 953–954, https://doi.org/10.1039/c39730000953, 1973.
Kaptein, R., Freeman, R., and Hill, H. D. W.: Carbon-13 CIDNP from
Biradicals in the Photolysis of Cyclic Ketones, Chem. Phys. Lett., 26,
104–107, https://doi.org/10.1016/0009-2614(74)89096-2, 1974.
Kaptein, R., van Leeuwen, P. W. N. M., and Huis, R.: CIDNP Study of
Homolytic Substitution (SH2) Reactions at Metal Centres, J. Chem. Soc. Chem. Comm., 568–569, https://doi.org/10.1039/c39750000568, 1975.
Kaptein, R., Dijkstra, K., and Nicolay, K.: Laser Photo-CIDNP as a Surface
Probe for Proteins in Solution, Nature, 274, 293–294, https://doi.org/10.1038/274293a0, 1978.
Kaptein, R., Nicolay, K., and Dijkstra, K.: Photo-CIDNP in Nucleic Acid
Bases and Nucleotides, J. Chem. Soc. Chem. Comm., 1092–1094, https://doi.org/10.1039/c39790001092, 1979.
Kaptein, R., Zuiderweg, E. R. P., Scheek, R. M., Boelens, R., and van
Gunsteren, W. F.: A Protein Structure from Nuclear Magnetic Resonance Data:
lac Repressor Headpiece, J. Mol. Biol., 182, 179–182,
https://doi.org/10.1016/0022-2836(85)90036-1, 1985.
Knegtel, R. M. A., Katahira, M., Schilthuis, J. G., Bonvin, A. M. J. J.,
Boelens, R., Eib, D., van der Saag, P. T., and Kaptein, R.: The solution
structure of the human retinoic acid receptor-beta DNA-binding domain, J.
Biomol. NMR, 3, 1–17, https://doi.org/10.1007/bf00242472, 1993.
Koning, T. M. G., Boelens, R., van der Marel, G. A., van Boom, J. H., and
Kaptein, R.: Structure determination of a DNA octamer in solution by NMR
spectroscopy. The effect of fast local motions, Biochemistry, 30, 3787–3797,
https://doi.org/10.1021/bi00229a028, 1991.
Lamerichs, R. M. J. N., Boelens, R., van der Marel, G. A., van Boom, J. H.,
Kaptein, R., Buck, F., Fera, B., and Rüterjans, H.: Proton NMR study of a complex between the lac repressor headpiece and a 22 base pair symmetric lac operator, Biochemistry, 28, 2985–2991, https://doi.org/10.1021/bi00433a037, 1989.
Laskowski, R. A., Rullmann, J. A. C., MacArthur, M. W., Kaptein, R., and
Thornton, J. M.: AQUA and PROCHECK-NMR: Programs for checking the quality of
protein structures solved by NMR, J. Biomol. NMR, 8, 477–486,
https://doi.org/10.1007/bf00228148, 1996.
Lehming, N., Sartorius, J., Niemöller, M., Genenger, G., von
Wilcken-Bergmann, B., and Müller-Hill, B.: The interaction of the
recognition helix of lac repressor with lac operator, EMBO J., 6, 3145–3153, https://doi.org/10.1002/j.1460-2075.1987.tb02625.x, 1987.
Lehming, N., Sartorius, J., Oehler, S., von Wilcken-Bergmann, B., and
Müller-Hill, B.: Recognition helices of lac and lambda repressor are
oriented in opposite directions and recognize similar DNA sequences, P. Natl. Acad. Sci. USA, 85, 7947–7951, https://doi.org/10.1073/pnas.85.21.7947, 1988.
Lenstra, J. A., Bolscher, B. G. J. M., Stob, S., Beintema, J. J., and
Kaptein, R.: The Aromatic Residues of Bovine Ribonuclease Studied by 1H Nuclear Magnetic Resonance, Eur. J. Biochem., 98, 385–397,
https://doi.org/10.1111/j.1432-1033.1979.tb13198.x, 1979.
Loth, K., Gnida, M., Romanuka, J., Kaptein, R., and Boelens, R.: Sliding and
target location of DNA-binding proteins:an NMR view of the lac repressor
system, J. Biomol. NMR, 56, 41–49, https://doi.org/10.1007/s10858-013-9723-0, 2013.
Marion, D., Driscoll, P. C., Kay, L. E., Wingfield, P. T., Bax, A.,
Gronenborn, A. M., and Clore, G. M.: Overcoming the overlap problem in the assignment of proton NMR spectra of larger proteins by use of three-dimensional heteronuclear proton-nitrogen-15 Hartmann-Hahn-multiple quantum coherence and nuclear Overhauser-multiple quantum coherence spectroscopy: application to interleukin 1.beta, Biochemistry, 28, 6150–6156, https://doi.org/10.1021/bi00441a004, 1989.
Markley, J. L., Bax, A., Arata, Y., Hilbers, C. W., Kaptein, R., Sykes, B.
D., Wright, P. E., and Wüthrich, K.: Recommendations for the
presentation of NMR structures of proteins and nucleic acids – (IUPAC
Recommendations 1998), Pure Appl. Chem., 70, 117–142,
https://doi.org/10.1351/pac199870010117, 1998.
Moonen, C. T. W., Hore, P. J., Müller, F., Kaptein, R., and Mayhew, S.
G.: A Photo-CIDNP Study of the active sites of Megashaera elsdenii and
Clostridium MP flavodoxins, FEBS Lett., 149, 141–146,
https://doi.org/10.1016/0014-5793(82)81090-9, 1982.
Morozova, O. B., Kiryutin, A. S., Sagdeev, R. Z., and Yurkovskaya, A. V.:
Electron transfer between guanosine radical and amino acids in aqueous
solution. 1. Reduction of guanosine radical by tyrosine, J. Phys. Chem. B, 111,
7439–7448, https://doi.org/10.1021/jp067722i, 2007.
Morozova, O. B., Kiryutin, A. S., and Yurkovskaya, A. V.: Electron transfer
between guanosine radicals and amino acids in aqueous solution. II.
Reduction of guanosine radicals by tryptophan, J. Phys. Chem. B, 112,
2747–2754, https://doi.org/10.1021/jp0752318, 2008.
Morozova, O. B., Kaptein, R., and Yurkovskaya, A. V.: Reduction of guanosyl
radical by cysteine and cysteine-glycine studied by time-resolved CIDNP, J.
Phys. Chem. B, 116, 8058–8063, https://doi.org/10.1021/jp301760b, 2012.
Morozova, O. B., Kaptein, R., Sagdeev, R. Z., and Yurkovskaya, A. V.:
Reduction of Guanosyl Radicals in Reactions with Proteins Studied by
TR-CIDNP, Appl. Magn. Reson., 44, 233–245, https://doi.org/10.1007/s00723-012-0403-0, 2013.
Nederveen, A. J., Doreleijers, J. F., Vranken, W., Miller, Z., Spronk, C. A.
E. M., Nabuurs, S. B., Güntert, P., Livny, M., Markley, J. L., Nilges,
M., Ulrich, E. L., Kaptein, R., and Bonvin, A. M. J. J.: RECOORD: A
recalculated coordinate database of 500+ proteins from the PDB using
restraints from the BioMagResBank, Proteins, 59, 662–672,
https://doi.org/10.1002/prot.20408, 2005.
Norton, R. S., Beress, L., Stob, S., Boelens, R., and Kaptein, R.:
Photochemically induced dynamic nuclear polarisation NMR study of the
aromatic residues of sea-anemone polypeptide cardiac stimulants, Eur. J.
Biochem., 157, 343–346, https://doi.org/10.1111/j.1432-1033.1986.tb09674.x, 1986.
Ohlendorf, D. H., Anderson, W. F., Fisher, R. G., Takeda, Y., and Matthews,
B. W.: The molecular basis of DNA-protein recognition inferred from the
structure of cro repressor, Nature, 298, 718–723, https://doi.org/10.1038/298718a0, 1982.
Pabo, C. O. and Lewis, M.: The operator-binding domain of lambda repressor:
structure and DNA recognition, Nature, 298, 443–447, https://doi.org/10.1038/298443a0, 1982.
Pravdivtsev, A. N., Ivanov, K. L., Kaptein, R., and Yurkovskaya, A. V.:
Theoretical Study of Dipolar Relaxation of Coupled Nuclear Spins at Variable
Magnetic Field, Appl. Magn. Reson., 44, 23–39, https://doi.org/10.1007/s00723-012-0404-z, 2013a.
Pravdivtsev, A. N., Yurkovskaya, A. V., Kaptein, R., Miesel, K., Vieth, H.
M., and Ivanov, K. L.: Exploiting level anti-crossings for efficient and
selective transfer of hyperpolarization in coupled nuclear spin systems,
Phys. Chem. Chem. Phys., 15, 14660–14669, https://doi.org/10.1039/c3cp52026a, 2013b.
Pravdivtsev, A. N., Ivanov, K. L., Yurkovskaya, A. V., Petrov, P. A.,
Limbach, H. H., Kaptein, R., and Vieth, H. M.: Spin polarization transfer
mechanisms of SABRE: A magnetic field dependent study, J. Magn. Reson., 261, 73–82, https://doi.org/10.1016/j.jmr.2015.10.006, 2015.
Redfield, C., Dobson, C. M., Scheek, R. M., Stob, S., and Kaptein, R.:
Surface accessibility of aromatic residues in human lysozyme using
photochemically induced dynamic nuclear polarization NMR spectroscopy, FEBS
Lett., 185, 248–252, https://doi.org/10.1016/0014-5793(85)80916-9, 1985.
Rubinstenn, G., Vuister, G. W., Mulder, F. A. A., Dux, P. E., Boelens, R.,
Hellingwerf, K. J., and Kaptein, R.: Structural and dynamic changes of
photoactive yellow protein during its photocycle in solution, Nat. Struct.
Biol., 5, 568–570, https://doi.org/10.1038/823, 1998.
Scheek, R. M., Kaptein, R., and Verhoeven, J. W.: Resolution of specific
histidine resonances in the 360 MHz 1H NMR spectrum of
glyceraldehyde-3-phosphate dehydrogenase, a 145 000 molecular weight protein, by photo-CIDNP, FEBS Lett., 107, 288–290,
https://doi.org/10.1016/0014-5793(79)80392-0, 1979.
Scheek, R. M., Russo, N., Boelens, R., and Kaptein, R.: Sequential resonance assignments in DNA proton NMR spectra by two-dimensional NOE spectroscopy, J. Am. Chem. Soc., 105, 2914–2916, https://doi.org/10.1021/ja00347a075, 1983.
Scheek, R. M., Boelens, R., Russo, N., van Boom, J. H., and Kaptein, R.:
Sequential resonance assignments in proton NMR spectra of oligonucleotides by two-dimensional NMR spectroscopy, Biochemistry, 23, 1371–1376,
https://doi.org/10.1021/bi00302a006, 1984.
Sette, M., van Tilborg, P. J. A., Spurio, R., Kaptein, R., Paci, M.,
Gualerzi, C. O., and Boelens, R.: The structure of the translational
initiation factor IF1 from E. coli contains an oligomer-binding motif, EMBO J., 16, 1436–1443, https://doi.org/10.1093/emboj/16.6.1436, 1997.
Siebert, H. C., Andre, S., Reuter, G., Gabius, H. J., Kaptein, R., and
Vliegenthart, J. F. G.: Effect of enzymatic desialylation of human serum
amyloid P component on surface exposure of laser photo CIDNP (chemically
induced dynamic nuclear polarization) – reactive histidine, tryptophan and
tyrosine residues, FEBS Lett., 371, 13–16, https://doi.org/10.1016/0014-5793(95)00845-z, 1995.
Siebert, H. C., Kaptein, R., Beintema, J. J., Soedjanaatmadja, U. M.,
Wright, C. S., Rice, A., Kleineidam, R. G., Kruse, S., Schauer, R., Pouwels,
P. J. W., Kamerling, J. P., Gabius, H. J., and Vliegenthart, J. F. G.:
Carbohydrate-protein interaction studies by laser photo CIDNP NMR methods,
Glycoconjugate J., 14, 531–534, https://doi.org/10.1023/a:1018572023153, 1997.
Spronk, C. A. E. M., Slijper, M., van Boom, J. H., Kaptein, R., and Boelens,
R.: Formation of the hinge helix in the lac repressor is induced upon
binding to the lac operator, Nat. Struct. Biol., 3, 916–919,
https://doi.org/10.1038/nsb1196-916, 1996.
Spronk, C. A. E. M., Folkers, G. E., Noordman, A. M. G. W., Wechselberger,
R., van den Brink, N., Boelens, R., and Kaptein, R.: Hinge-helix formation
and DNA bending in various lac repressor-operator complexes, The EMBO J., 18, 6472–6480, https://doi.org/10.1093/emboj/18.22.6472, 1999.
Tripsianes, K., Folkers, G., AB, E., Das, D., Odijk, H., Jaspers, N. G. J.,
Hoeijmakers, J. H. J., Kaptein, R., and Boelens, R.: The structure of the
human ERCC1/XPF interaction domains reveals a complementary role for the two
proteins in nucleotide excision repair, Structure, 13, 1849–1858,
https://doi.org/10.1016/j.str.2005.08.014, 2005.
van den Berg, B., Tessari, M., Boelens, R., Dijkman, R., de Haas, G. H.,
Kaptein, R., and Verheij, H. M.: NMR structures of phospholipase A2 reveal
conformational changes during interfacial activation, Nat. Struct. Biol., 2,
402–406, https://doi.org/10.1038/nsb0595-402, 1995a.
van den Berg, B., Tessari, M., Boelens, R., Dijkman, R., Kaptein, R., de
Haas, G. H., and Verheij, H. M.: Solution structure of porcine pancreatic
phospholipase A2 complexed with micelles and a competitive inhibitor, J.
Biomol. NMR, 5, 110–121, https://doi.org/10.1007/bf00208802, 1995b.
van der Horst, M. A., van Stokkum, I. H., Crielaard, W., and Hellingwerf, K.
J.: The role of the N-terminal domain of photoactive yellow protein in the
transient partial unfolding during signalling state formation, FEBS Lett.,
497, 26–30, https://doi.org/10.1016/s0014-5793(01)02427-9, 2001.
van der Waals, J. and Hilbers, K.: Moleculen doorgrond: kwantumchemie en
spectroscopie, in: De geschiedenis van de scheikunde in Nederland 3, De
ontwikkeling van de chemie van 1945 tot het begin van de jaren tachtig,
Delft University Press, Delft, 105–129, 2004.
van Gunsteren, W. F., Kaptein, R., and Zuiderweg, E. R. P.: Use of molecular
dynamics computer simulations when determining protein structure by 2D-NMR,
in: Proceedings of the NATO/CECAM Workshop on Nucleic Acid Conformation and
Dynamics, edited by: Olsen, W. K., Centre de Calcul Atomique et Moleculaire,
Orsay, 79–82, 1984.
van Leeuwen, P. W. N. M., Kaptein, R., Huis, R., and Kalisvaart, W. I.:
CIDNP Studies of Reactions of Alkyllead compounds with Hexachloroacetone and
Hexachlorocyclopentadiene, J. Organomet. Chem., 93, C5–C7,
https://doi.org/10.1016/s0022-328x(00)94154-8, 1975.
Vis, H., Mariani, M., Vorgias, C. E., Wilson, K. S., Kaptein, R., and
Boelens, R.: Solution structure of the HU protein from Bacillus stearothermophilus, J. Mol. Biol., 254, 692–703, https://doi.org/10.1006/jmbi.1995.0648, 1995.
von Hippel, P. H. and Berg, O. G.: Facilitated target location in
biological systems, J. Biol. Chem., 264, 675–678,
https://doi.org/10.1016/S0021-9258(19)84994-3, 1989.
Vuister, G. W. and Boelens, R.: Three-dimensional J-resolved NMR spectroscopy, J. Magn. Reson., 73, 328–333, https://doi.org/10.1016/0022-2364(87)90205-8, 1987.
Vuister, G. W., Boelens, R., and Kaptein, R.: Non-selective
three-dimensional NMR spectroscopy. The 3D NOE-HOHAHA experiment, J. Magn. Reson., 80, 176–185, https://doi.org/10.1016/0022-2364(88)90072-8, 1988.
Ward, H. R. and Lawler, R. G.: Nuclear magnetic resonance emission and
enhanced absorption in rapid organometallic reactions, J. Am. Chem. Soc.,
89, 5518–5519, https://doi.org/10.1021/ja00997a078, 1967.
Zetta, L., Kaptein, R., and Hore, P. J.: A Photo-CIDNP investigation of
tyrosine mobility and exposure in human beta-endorphin in the presence of
phospholipid micelles, FEBS Lett., 145, 277–280,
https://doi.org/10.1016/0014-5793(82)80182-8, 1982.
Zetta, L., Böhmer, V., and Kaptein, R.: Rapid hydrogen atom transfer in
oligophenols. A photo-CIDNP study, J. Magn. Reson., 76, 587–591, https://doi.org/10.1016/0022-2364(88)90363-0, 1988.
Zuiderweg, E. R. P. and Fesik, S. W.: Heteronuclear three-dimensional NMR
spectroscopy of the inflammatory protein C5a, Biochemistry, 28, 2387–2391,
https://doi.org/10.1021/bi00432a008, 1989.
Zuiderweg, E. R. P., Kaptein, R., and Wüthrich, K.: Secondary structure
of the lac repressor DNA-binding domain by two-dimensional 1H nuclear magnetic resonance in solution, P. Natl. Acad. Sci.-Biol., 80, 5837–5841,
https://doi.org/10.1073/pnas.80.19.5837, 1983a.
Zuiderweg, E. R. P., Kaptein, R., and Wüthrich, K.: Sequence-specific
resonance assignments in the 1H nuclear-magnetic-resonance spectrum of the Lac repressor DNA-binding domain 1–51 from Escherichia coli by two-dimensional spectroscopy, Eur. J. Biochem., 137, 279–292,
https://doi.org/10.1111/j.1432-1033.1983.tb07827.x, 1983b.
Zuiderweg, E. R. P., Scheek, R. M., Boelens, R., van Gunsteren, W. F., and
Kaptein, R.: Determination of protein structures from nuclear magnetic
resonance data using a restrained molecular dynamics approach: The lac
repressor DNA binding domain, Biochimie, 67, 707–715,
https://doi.org/10.1016/s0300-9084(85)80158-9, 1985.
Short summary
This publication presents research in biomolecular NMR, spin hyperpolarisation and spin chemistry. Robert Kaptein made key contributions to magnetic resonance and proposed the radical pair mechanism for chemically induced dynamic nuclear polarisation (CIDNP). He developed laser CIDNP and computational methods for protein structure determination. He is known for studying the lac repressor and its DNA complexes. He played a leading role in establishing the NMR large-scale facilities in Europe.
This publication presents research in biomolecular NMR, spin hyperpolarisation and spin...
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