PUBLICATIONS:

Ph.D. thesis:

  1. Duin, E.C. (1996) Exploring the active site of nickel-hydrogenases. University of Amsterdam, Amsterdam, Copy 2000, Enschede, The Netherlands.

Book chapters:

  1. Johnson, M.K., Duin, E.C., Crouse, B.R., Gollinelli, M.-P., and Meyer, J. (1997) Valence-delocalized [Fe2S2]+ clusters. ACS Symposium Series 692, Spectroscopic Methods in Bioinorganic Chemistry, Eds. Solomon, E.I. and Hodgson, K.O., pp. 286-301.

  2. Johnson, M.K., Duderstadt, R.E., and Duin, E.C. (1999) Biological and synthetic [Fe3S4] clusters. Adv. Inorg. Chem., 47, 1-82.

  3. Grabarse, W., Shima, S., Mahlert, F., Duin, E.C., Thauer, R.K., and Ermler, U. (2001) Methyl-coenzyme M reductase. In: Handbook of Metalloproteins, Volume 2 (Eds. Wieghardt, K., Huber, R., Poulos, T.L., Messerschmidt, A.), John Wiley & Sons, Chichester, pp. 897-914.

  4. Duin, E.C., (2008) Role of coenzyme F430 in methanogenesis. In: Tetrapyrroles: their birth, life and death, (Eds. Warren, M.J., Smith, A.), Landes Bioscience, Georgetown, Online.

Articles in refereed journals:

  1. Surerus, K.K., Chen, M., Van der Zwaan, J.W., Rusnak, F.M., Kolk, M., Duin, E.C., Albracht, S.P.J., and Münck, E. (1994) Further characterization of the spin coupling observed in oxidized hydrogenase from Chromatium vinosum. A Mössbauer and multifrequency EPR study. Biochemistry, 33, 4980-4993. Abstract - PDF (Full)

  2. Bagley, K.A., Van Garderen, C.J., Chen, M., Duin, E.C., Albracht, S.P.J., and Woodruff, W.H. (1994) Infrared studies on the interaction of carbon monoxide with divalent nickel in hydrogenase from Chromatium vinosum. Biochemistry, 33, 9229-9236. Abstract - PDF (Full)

  3. Bagley, K.A., Duin, E.C., Roseboom, W., Albracht, S.P.J., and Woodruff, W.H. (1995) An infrared-detectable group senses changes in charge density on the nickel center in hydrogenase from Chromatium vinosum. Biochemistry, 34, 5527-5535. Abstract - PDF (Full)

  4. Sorgenfrei, O., Duin, E.C., Klein, A., and Albracht, S.P.J. (1996) Interactions of 77Se and 13CO with nickel in the active site of active F420-nonreducing hydrogenase from Methanococcus voltae. J. Biol. Chem., 271, 23799-23806. Abstract/Full

  5. Saal, C., Mohanta, S., Nag, K., Dutta, S.K., Werner, R., Haase, W., Duin, E., and Johnson, M.K. (1996) Magnetic investigations on a valence-delocalized dinuclear Fe(II)-Fe(III) complex. Ber. Bunsenges. Phys. Chem., 100, 2086-2090. Abstract

  6. Sorgenfrei, O., Duin, E.C., Klein, A., and Albracht, S.P.J. (1997) Changes in the electronic structure around Ni in oxidized and reduced selenium-containing hydrogenases from Methanococcus voltae. Eur. J. Biochem., 247, 681-687. Abstract/Full

  7. Duin, E.C., Lafferty, M.E., Crouse, B.R., Allen, R.M., Sanyal, I., Flint, D.H., and Johnson, M.K. (1997) [2Fe-2S] to [4Fe-4S] cluster conversion in Escherichia coli biotin synthase. Biochemistry, 36, 11811-11820. Abstract/Full

  8. Johnson, M.K., Staples, C.R., Duin, E.C., Lafferty, M.E., and Duderstadt, R.E. (1998) Novel roles for Fe-S clusters in stabilizing or generating radical intermediates. Pure and Applied Chemistry, 70, 939-946. Abstract

  9. Golinelli, M.-P., Chatelet, C., Duin, E.C., Johnson, M.K., and Meyer, J. (1998) Extensive ligand rearrangements around the [2Fe-2S] cluster of Clostridium pasteurianum ferredoxin. Biochemistry, 37, 10429-10437. Abstract/Full

  10. Pershad, H.R., Duff, J.L.C., Heering, H.A., Duin, E.C., Albracht, S.P.J., and Armstrong, F.A. (1999) Catalytic electron transport in Chromatium vinosum [NiFe]-hydrogenase: Application of voltammetry in detecting redox-active centers and establishing that hydrogen oxidation is very fast even at potentials close to the reversible H+/H2 value. Biochemistry, 38, 8992-8999. Abstract/Full

  11. Wastl, J., Duin, E.C., Iuzzolino, L., Dörner, W., Link, T., Hoffmann, S., Sticht, H., Dau, H., Lingelbach, K., and Maier, U.-G. (2000) Eukaryotically encoded and chloroplast-located rubredoxin is associated with photosystem II. J. Biol. Chem., 275, 30058-30063. Abstract/Full

  12. Grabarse, W, Mahlert, F., Duin, E.C., Goubeaud, M., Shima, S., Thauer, R.K., Lamzin, V., and Ermler, U. (2001) On the mechanism of biological methane formation: Structural evidence for conformational changes in methyl-coenzyme M reductase upon substrate binding. J. Mol. Biol., 309, 315-330. Abstract/Full

  13. Madadi Kahkesh, S., Duin, E.C., Heim, S., Albracht, S.P.J., Johnson, M.K., and Hedderich, R. (2001) A paramagnetic species with unique EPR characteristics in the active site of heterodisulfide reductase from methanogenic archaea. Eur. J. Biochem., 268, 2566-2577. Abstract/Full

  14. Mahlert, F., Grabarse, W., Kahnt, J., Thauer, R.K., and Duin, E.C. (2002) The nickel enzyme methyl-coenzyme M reductase from methanogenic archaea: in vitro induction of the nickel based and light sensitive EPR-red2 signal by coenzyme M plus coenzyme B. J. Biol. Inorg. Chem., 7, 101-112 & 7, 351. Abstract/Full

  15. Duin, E.C., Madadi-Kahkesh, S., Hedderich, R., Clay, M.D., and Johnson, M.K. (2002) Heterodisulfide reductase from Methanothermobacter marburgensis contains an active-site [4Fe-4S] cluster that is directly involved in mediating heterodisulfide reduction. FEBS Lett., 512, 263-268. Abstract/Full

  16. Mahlert, F., Bauer, C., Jaun, B., Thauer, R.K., and Duin, E.C. (2002) The nickel enzyme methyl-coenzyme M reductase from methanogenic archaea: in vitro induction of the nickel based MCR-ox EPR signals from MCR-red2. J. Biol. Inorg. Chem., 7, 500-513. Abstract/Full

  17. Mander, G.J., Duin, E.C., Linder, D., Stetter, K.O., and Hedderich, R. (2002) Purification and characterization of a membrane-bound enzyme complex from the sulfate-reducing archaeon Archaeoglobus fulgidus related to heterodisulfide reductase from methanogenic archaea. Eur. J. Biochem., 269, 1895-1904. Abstract/Full

  18. Kollas, A.-K, Duin, E.C., Eberl, M., Altincicek, B., Hintz, M., Reichenberg, A., Henschker, D., Henne, A., Steinbrecher, I., Ostrovsky, D.N., Hedderich, R., Beck, E., Jomaa, H., Wiesner, J. (2002) Functional characterization of GcpE, an essential enzyme of the non-mevalonate pathway of isoprenoid biosynthesis. FEBS Lett., 532, 432-436. Abstract/Full

  19. Altincicek, B., Duin, E.C., Reichenberg, A., Hedderich, R., Kollas, A.-K., Hintz, M., Wagner, S., Wiesner, J., Beck, E., Jomaa, H. (2002) LytB protein catalyzes the terminal step of the 2-C-methyl-D-erythritol-4-phosphate pathway of isoprenoid biosynthesis. FEBS Lett., 532, 437-440. Abstract/Full

  20. Duin, E.C., Cosper, N.J., Mahlert, F., Thauer, R.K., Scott, R.A. (2003) Coordination and geometry of the nickel atom in active methyl-coenzyme M reductase from Methanothermobacter marburgensis as detected by X-ray absorption spectroscopy. J. Biol. Inorg. Chem., 8, 141-148. Abstract/Full

  21. Duin, E.C., Bauer, C., Jaun, B., Hedderich, R. (2003) Coenzyme M binds to a [4Fe-4S] cluster in the active site of heterodisulfide reductase as deduced from EPR studies with the [33S]coenzyme treated enzyme. FEBS Lett., 538, 81-84. Abstract/Full

  22. Finazzo, C., Harmer, J., Jaun, B., Duin, E.C., Mahlert, F., Thauer, R.K., Van Doorslaer, S., Schweiger, A. (2003) Characterization of the MCRred2 form of Methyl-Coenzyme M reductase, a pulse EPR and ENDOR study. J. Biol. Inorg. Chem., 8, 586-593. Abstract/Full

  23. Finazzo, C., Harmer, J., Bauer, C., Jaun, B., Duin, E.C., Mahlert, F., Goenrich, M., Thauer, R.K., Van Doorslaer, S., Schweiger, A. (2003) Coenzyme B induced coordination of methyl coenzyme M via its thiol group to Ni(I) of F430 in active methyl-coenzyme M reductase. J. Am. Chem. Soc., 125, 4988-4989. Abstract/Full

  24. Stojanowic, A., Mander, G.J., Duin, E.C., Hedderich, R. (2003) Physiological role of the F420-non reducing hydrogenase (Mvh) from Methanothermobacter marburgensis. Arch. Microbiol., 180, 194-203. Abstract/Full

  25. Duin, E.C., Signor, L., Piskorski, R., Mahlert, F., Clay, M.D., Goenrich, M., Thauer, R.K., Jaun, B., Johnson, M.K. (2004) Spectroscopic investigation of the nickel-containing porphinoid cofactor F430. Comparison of the free cofactor in the +1, +2 and +3 oxidation states with the cofactor bound to methyl coenzyme M reductase in the silent, red and ox forms. J. Biol. Inorg. Chem., 9, 563-576. Abstract/Full

  26. Goenrich, M., Mahlert, F., Duin, E.C., Bauer, C., Jaun, B., Thauer, R.K. (2004) Probing the reactivity of Ni in the active site of methyl-coenzyme M reductase with substrate analogues. J. Biol. Inorg. Chem., 9, 691-705. Abstract/Full

  27. Goenrich, M., Duin, E.C., Mahlert, F., Thauer, R.K. (2005) Temperature dependence of methyl-coenzyme M reductase (MCR) activity and the formation of the MCR-red2 state induced by coenzyme B. J. Biol. Inorg. Chem., 10, 333-342. Abstract/Full

  28. Shokes, J.E., Duin, E.C., Bauer, C., Jaun, B., Hedderich, R., Koch, J., Scott, R.A. (2005) Direct interaction of coenzyme M with the active-site Fe-S cluster of heterodisulfide reductase. FEBS Lett., 579, 1741-1744. Abstract/Full

  29. Harmer, J., Finazzo, C., Piskorski, R., Bauer, C., Jaun, B., Duin, E.C., Goenrich, M., Thauer, R.K., van Doorslaer, S., Schweiger, A. (2005) Spin density and coenzyme M coordination geometry of the ox1 form of methyl-coenzyme M reductase: A pulse EPR study. J. Am. Chem. Soc., 127, 17744-17755. Abstract/Full

  30. Shvareva, T.Y., Beitz, J.V., Duin, E.C., Albrecht-Schmitt, T.E. (2005) Polar open-framework structure, optical properties, and electron paramagnetic resonance of the mixed-metal uranyl phosphate Cs2[UO2(VO2)2(PO4)2]∙0.59H2O. Chem. Mater., 17, 6219-6222. Abstract/Full

  31. Adedeji, D., Hernandez, H., Wiesner, J., Köhler, U., Jomaa, H., Duin, E.C. (2007) Possible direct involvement of the active-site [4Fe-4S] cluster of the GcpE enzyme from Thermus thermophilus in the conversion of MEcPP. FEBS Lett., 581, 279-283. Abstract/Full

  32. Yang, N., Reiher, M., Wang, M., Harmer, J., Duin, E.C. (2007) Formation of a nickel-methyl species in methyl-coenzyme M reductase, an enzyme catalyzing methane formation. J. Am. Chem. Soc., 129, 11028-11029. Abstract/Full

  33. Narayanan, A., Ramamurthy, V., Duin, E., Thakur, M. (2008) EPR spectroscopic studies of radical cations in a novel nonconjugated conductive polymer, poly(β-pinene). J. Macromol. Sci., Pure Appl. Chem., 45, 195-198. Abstract/Full