| Year |
Citation |
Score |
| 2024 |
Ghebreamlak S, Stoian SA, Lees NS, Cronin B, Smith F, Ross MO, Telser J, Hoffman BM, Duin EC. The Active-Site [4Fe-4S] Cluster in the Isoprenoid Biosynthesis Enzyme IspH Adopts Unexpected Redox States during Ligand Binding and Catalysis. Journal of the American Chemical Society. PMID 38291562 DOI: 10.1021/jacs.3c11674 |
0.582 |
|
| 2022 |
Gencic S, Duin EC, Grahame DA. The two-electron reduced A cluster in acetyl-CoA synthase: Preparation, characteristics and mechanistic implications. Journal of Inorganic Biochemistry. 240: 112098. PMID 36580832 DOI: 10.1016/j.jinorgbio.2022.112098 |
0.476 |
|
| 2020 |
Deere TM, Prakash D, Lessner FH, Duin EC, Lessner DJ. Methanosarcina acetivorans contains a functional ISC system for iron-sulfur cluster biogenesis. Bmc Microbiology. 20: 323. PMID 33096982 DOI: 10.1186/s12866-020-02014-z |
0.439 |
|
| 2019 |
Lyu Z, Shao N, Chou CW, Shi H, Patel R, Duin EC, Whitman WB. Post-translational methylation of arginine in methyl-coenzyme M reductase has a profound impact on both methanogenesis and growth of . Journal of Bacteriology. PMID 31740491 DOI: 10.1128/Jb.00654-19 |
0.405 |
|
| 2018 |
Lyu Z, Chou CW, Shi H, Wang L, Ghebreab R, Phillips D, Yan Y, Duin EC, Whitman WB. Assembly of methyl-coenzyme M reductase in the methanogenic archaeon Methanococcus maripaludis. Journal of Bacteriology. PMID 29339414 DOI: 10.1128/Jb.00746-17 |
0.366 |
|
| 2016 |
Duin EC, Wagner T, Shima S, Prakash D, Cronin B, Yáñez-Ruiz DR, Duval S, Rümbeli R, Stemmler RT, Thauer RK, Kindermann M. Mode of action uncovered for the specific reduction of methane emissions from ruminants by the small molecule 3-nitrooxypropanol. Proceedings of the National Academy of Sciences of the United States of America. PMID 27140643 DOI: 10.1073/Pnas.1600298113 |
0.395 |
|
| 2015 |
Subramanian S, Duin EC, Fawcett SE, Armstrong FA, Meyer J, Johnson MK. Spectroscopic and redox studies of valence-delocalized [Fe2S2](+) centers in thioredoxin-like ferredoxins. Journal of the American Chemical Society. 137: 4567-80. PMID 25790339 DOI: 10.1021/Jacs.5B01869 |
0.523 |
|
| 2014 |
Prakash D, Wu Y, Suh SJ, Duin EC. Elucidating the process of activation of methyl-coenzyme M reductase. Journal of Bacteriology. 196: 2491-8. PMID 24769699 DOI: 10.1128/Jb.01658-14 |
0.493 |
|
| 2013 |
Gencic S, Kelly K, Ghebreamlak S, Duin EC, Grahame DA. Different modes of carbon monoxide binding to acetyl-CoA synthase and the role of a conserved phenylalanine in the coordination environment of nickel. Biochemistry. 52: 1705-16. PMID 23394607 DOI: 10.1021/Bi3016718 |
0.53 |
|
| 2012 |
Xu W, Lees NS, Hall D, Welideniya D, Hoffman BM, Duin EC. A closer look at the spectroscopic properties of possible reaction intermediates in wild-type and mutant (E)-4-hydroxy-3-methylbut-2-enyl diphosphate reductase. Biochemistry. 51: 4835-49. PMID 22646150 DOI: 10.1021/Bi3001215 |
0.651 |
|
| 2012 |
Lessner FH, Jennings ME, Hirata A, Duin EC, Lessner DJ. Subunit D of RNA polymerase from Methanosarcina acetivorans contains two oxygen-labile [4Fe-4S] clusters: implications for oxidant-dependent regulation of transcription. The Journal of Biological Chemistry. 287: 18510-23. PMID 22457356 DOI: 10.1074/Jbc.M111.331199 |
0.409 |
|
| 2011 |
Duin EC, Prakash D, Brungess C. Methyl-coenzyme M reductase from Methanothermobacter marburgensis. Methods in Enzymology. 494: 159-87. PMID 21402215 DOI: 10.1016/B978-0-12-385112-3.00009-3 |
0.35 |
|
| 2011 |
Dhage P, Samokhvalov A, Repala D, Duin EC, Tatarchuk BJ. Regenerable Fe-Mn-ZnO/SiO2 sorbents for room temperature removal of H2S from fuel reformates: performance, active sites, Operando studies. Physical Chemistry Chemical Physics : Pccp. 13: 2179-87. PMID 21132188 DOI: 10.1039/C0Cp01355B |
0.409 |
|
| 2010 |
Xu W, Lees NS, Adedeji D, Wiesner J, Jomaa H, Hoffman BM, Duin EC. Paramagnetic intermediates of (E)-4-hydroxy-3-methylbut-2-enyl diphosphate synthase (GcpE/IspG) under steady-state and pre-steady-state conditions. Journal of the American Chemical Society. 132: 14509-20. PMID 20863107 DOI: 10.1021/Ja101764W |
0.662 |
|
| 2010 |
Gencic S, Duin EC, Grahame DA. Tight coupling of partial reactions in the acetyl-CoA decarbonylase/synthase (ACDS) multienzyme complex from Methanosarcina thermophila: acetyl C-C bond fragmentation at the a cluster promoted by protein conformational changes. The Journal of Biological Chemistry. 285: 15450-63. PMID 20202935 DOI: 10.1074/Jbc.M109.080994 |
0.504 |
|
| 2009 |
Jambovane S, Duin EC, Kim SK, Hong JW. Determination of kinetic parameters, Km and kcat, with a single experiment on a chip. Analytical Chemistry. 81: 3239-45. PMID 19338287 DOI: 10.1021/Ac8020938 |
0.367 |
|
| 2008 |
Rekittke I, Wiesner J, Röhrich R, Demmer U, Warkentin E, Xu W, Troschke K, Hintz M, No JH, Duin EC, Oldfield E, Jomaa H, Ermler U. Structure of (E)-4-hydroxy-3-methyl-but-2-enyl diphosphate reductase, the terminal enzyme of the non-mevalonate pathway. Journal of the American Chemical Society. 130: 17206-7. PMID 19035630 DOI: 10.1021/Ja806668Q |
0.518 |
|
| 2008 |
Harmer J, Finazzo C, Piskorski R, Ebner S, Duin EC, Goenrich M, Thauer RK, Reiher M, Schweiger A, Hinderberger D, Jaun B. A nickel hydride complex in the active site of methyl-coenzyme m reductase: implications for the catalytic cycle. Journal of the American Chemical Society. 130: 10907-20. PMID 18652465 DOI: 10.1021/Ja710949E |
0.472 |
|
| 2008 |
Duin EC, McKee ML. A new mechanism for methane production from methyl-coenzyme M reductase as derived from density functional calculations. The Journal of Physical Chemistry. B. 112: 2466-82. PMID 18247503 DOI: 10.1021/Jp709860C |
0.417 |
|
| 2007 |
Yang N, Reiher M, Wang M, Harmer J, Duin EC. Formation of a nickel-methyl species in methyl-coenzyme m reductase, an enzyme catalyzing methane formation. Journal of the American Chemical Society. 129: 11028-9. PMID 17711279 DOI: 10.1021/Ja0734501 |
0.622 |
|
| 2007 |
Adedeji D, Hernandez H, Wiesner J, Köhler U, Jomaa H, Duin EC. Possible direct involvement of the active-site [4Fe-4S] cluster of the GcpE enzyme from Thermus thermophilus in the conversion of MEcPP. Febs Letters. 581: 279-83. PMID 17214985 DOI: 10.1016/J.Febslet.2006.12.026 |
0.665 |
|
| 2005 |
Harmer J, Finazzo C, Piskorski R, Bauer C, Jaun B, Duin EC, Goenrich M, Thauer RK, Van Doorslaer S, Schweiger A. Spin density and coenzyme M coordination geometry of the ox1 form of methyl-coenzyme M reductase: a pulse EPR study. Journal of the American Chemical Society. 127: 17744-55. PMID 16351103 DOI: 10.1021/Ja053794W |
0.395 |
|
| 2005 |
Goenrich M, Duin EC, Mahlert F, Thauer RK. Temperature dependence of methyl-coenzyme M reductase activity and of the formation of the methyl-coenzyme M reductase red2 state induced by coenzyme B. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 10: 333-42. PMID 15846525 DOI: 10.1007/S00775-005-0636-6 |
0.471 |
|
| 2005 |
Shokes JE, Duin EC, Bauer C, Jaun B, Hedderich R, Koch J, Scott RA. Direct interaction of coenzyme M with the active-site Fe-S cluster of heterodisulfide reductase. Febs Letters. 579: 1741-4. PMID 15757669 DOI: 10.1016/J.Febslet.2005.02.034 |
0.596 |
|
| 2004 |
Goenrich M, Mahlert F, Duin EC, Bauer C, Jaun B, Thauer RK. Probing the reactivity of Ni in the active site of methyl-coenzyme M reductase with substrate analogues. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 9: 691-705. PMID 15365904 DOI: 10.1007/S00775-004-0552-1 |
0.444 |
|
| 2004 |
Duin EC, Signor L, Piskorski R, Mahlert F, Clay MD, Goenrich M, Thauer RK, Jaun B, Johnson MK. Spectroscopic investigation of the nickel-containing porphinoid cofactor F(430). 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. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 9: 563-76. PMID 15160314 DOI: 10.1007/S00775-004-0549-9 |
0.441 |
|
| 2003 |
Stojanowic A, Mander GJ, Duin EC, Hedderich R. Physiological role of the F420-non-reducing hydrogenase (Mvh) from Methanothermobacter marburgensis. Archives of Microbiology. 180: 194-203. PMID 12856108 DOI: 10.1007/S00203-003-0577-9 |
0.516 |
|
| 2003 |
Finazzo C, Harmer J, Bauer C, Jaun B, Duin EC, Mahlert F, Goenrich M, Thauer RK, Van Doorslaer S, Schweiger A. Coenzyme B induced coordination of coenzyme M via its thiol group to Ni(I) of F430 in active methyl-coenzyme M reductase. Journal of the American Chemical Society. 125: 4988-9. PMID 12708843 DOI: 10.1021/Ja0344314 |
0.437 |
|
| 2003 |
Duin EC, Bauer C, Jaun B, Hedderich R. Coenzyme M binds to a [4Fe-4S] cluster in the active site of heterodisulfide reductase as deduced from EPR studies with the [33S]coenzyme M-treated enzyme. Febs Letters. 538: 81-4. PMID 12633857 DOI: 10.1016/S0014-5793(03)00134-0 |
0.634 |
|
| 2003 |
Finazzo C, Harmer J, Jaun B, Duin EC, Mahlert F, Thauer RK, Van Doorslaer S, Schweiger A. Characterization of the MCRred2 form of methyl-coenzyme M reductase: a pulse EPR and ENDOR study. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 8: 586-93. PMID 12624730 DOI: 10.1007/S00775-003-0450-Y |
0.472 |
|
| 2003 |
Duin EC, Cosper NJ, Mahlert F, Thauer RK, Scott RA. Coordination and geometry of the nickel atom in active methyl-coenzyme M reductase from Methanothermobacter marburgensis as detected by X-ray absorption spectroscopy. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 8: 141-8. PMID 12459909 DOI: 10.1007/S00775-002-0399-2 |
0.446 |
|
| 2002 |
Altincicek B, Duin EC, Reichenberg A, Hedderich R, Kollas AK, Hintz M, Wagner S, Wiesner J, Beck E, Jomaa H. LytB protein catalyzes the terminal step of the 2-C-methyl-D-erythritol-4-phosphate pathway of isoprenoid biosynthesis. Febs Letters. 532: 437-40. PMID 12482608 DOI: 10.1016/S0014-5793(02)03726-2 |
0.378 |
|
| 2002 |
Kollas AK, Duin EC, Eberl M, Altincicek B, Hintz M, Reichenberg A, Henschker D, Henne A, Steinbrecher I, Ostrovsky DN, Hedderich R, Beck E, Jomaa H, Wiesner J. Functional characterization of GcpE, an essential enzyme of the non-mevalonate pathway of isoprenoid biosynthesis. Febs Letters. 532: 432-6. PMID 12482607 DOI: 10.1016/S0014-5793(02)03725-0 |
0.436 |
|
| 2002 |
Mander GJ, Duin EC, Linder D, Stetter KO, Hedderich R. Purification and characterization of a membrane-bound enzyme complex from the sulfate-reducing archaeon Archaeoglobus fulgidus related to heterodisulfide reductase from methanogenic archaea. European Journal of Biochemistry / Febs. 269: 1895-904. PMID 11952791 DOI: 10.1046/J.1432-1033.2002.02839.X |
0.499 |
|
| 2002 |
Mahlert F, Bauer C, Jaun B, Thauer RK, Duin EC. The nickel enzyme methyl-coenzyme M reductase from methanogenic archaea: In vitro induction of the nickel-based MCR-ox EPR signals from MCR-red2. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 7: 500-13. PMID 11941508 DOI: 10.1007/S00775-001-0325-Z |
0.486 |
|
| 2002 |
Mahlert F, Grabarse W, Kahnt J, Thauer RK, Duin EC. The nickel enzyme methyl-coenzyme M reductase from methanogenic archaea: in vitro interconversions among the EPR detectable MCR-red1 and MCR-red2 states. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 7: 101-12. PMID 11862546 DOI: 10.1007/S007750100270 |
0.464 |
|
| 2002 |
Duin EC, Madadi-Kahkesh S, Hedderich R, Clay MD, Johnson MK. Heterodisulfide reductase from Methanothermobacter marburgensis contains an active-site [4Fe-4S] cluster that is directly involved in mediating heterodisulfide reduction. Febs Letters. 512: 263-8. PMID 11852093 DOI: 10.1016/S0014-5793(02)02281-0 |
0.595 |
|
| 2001 |
Grabarse W, Mahlert F, Duin EC, Goubeaud M, Shima S, Thauer RK, Lamzin V, Ermler U. On the mechanism of biological methane formation: structural evidence for conformational changes in methyl-coenzyme M reductase upon substrate binding. Journal of Molecular Biology. 309: 315-30. PMID 11491299 DOI: 10.1006/Jmbi.2001.4647 |
0.458 |
|
| 2001 |
Madadi-Kahkesh S, Duin EC, Heim S, Albracht SP, Johnson MK, Hedderich R. A paramagnetic species with unique EPR characteristics in the active site of heterodisulfide reductase from methanogenic archaea. European Journal of Biochemistry / Febs. 268: 2566-77. PMID 11322875 DOI: 10.1046/J.1432-1327.2001.02141.X |
0.554 |
|
| 2000 |
Wastl J, Duin EC, Iuzzolino L, Dörner W, Link T, Hoffmann S, Sticht H, Dau H, Lingelbach K, Maier UG. Eukaryotically encoded and chloroplast-located rubredoxin is associated with photosystem II. The Journal of Biological Chemistry. 275: 30058-63. PMID 10878021 DOI: 10.1074/Jbc.M004629200 |
0.306 |
|
| 1999 |
Pershad HR, Duff JL, Heering HA, Duin EC, Albracht SP, Armstrong FA. 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: 8992-9. PMID 10413472 DOI: 10.1021/Bi990108V |
0.51 |
|
| 1999 |
Johnson MK, Duderstadt RE, Duin EC. Biological and Synthetic [Fe3S4] Clusters Advances in Inorganic Chemistry. 47: 1-82. DOI: 10.1016/S0898-8838(08)60076-8 |
0.431 |
|
| 1998 |
Golinelli MP, Chatelet C, Duin EC, Johnson MK, Meyer J. Extensive ligand rearrangements around the [2Fe-2S] cluster of Clostridium pasteurianum ferredoxin. Biochemistry. 37: 10429-37. PMID 9671512 DOI: 10.1021/Bi9806394 |
0.514 |
|
| 1998 |
Johnson MK, Staples CR, Duin EC, Lafferty ME, Duderstadt RE. Novel roles for Fe-S clusters in stabilizing or generating radical intermediates Pure and Applied Chemistry. 70: 939-946. DOI: 10.1351/Pac199870040939 |
0.61 |
|
| 1998 |
Johnson MK, Duin EC, Crouse BR, Golinelli MP, Meyer J. Valence-Delocalized [Fe2S2]+ Clusters Acs Symposium Series. 692: 286-301. |
0.425 |
|
| 1997 |
Duin EC, Lafferty ME, Crouse BR, Allen RM, Sanyal I, Flint DH, Johnson MK. [2Fe-2S] to [4Fe-4S] cluster conversion in Escherichia coli biotin synthase. Biochemistry. 36: 11811-20. PMID 9305972 DOI: 10.1021/Bi9706430 |
0.58 |
|
| 1997 |
Sorgenfrei O, Duin EC, Klein A, Albracht SP. Changes in the electronic structure around Ni in oxidized and reduced selenium-containing hydrogenases from Methanococcus voltae. European Journal of Biochemistry / Febs. 247: 681-7. PMID 9266713 DOI: 10.1111/J.1432-1033.1997.00681.X |
0.428 |
|
| 1996 |
Sorgenfrei O, Duin EC, Klein A, Albracht SP. Interactions of 77Se and 13CO with nickel in the active site of active F420-nonreducing hydrogenase from Methanococcus voltae. The Journal of Biological Chemistry. 271: 23799-806. PMID 8798608 DOI: 10.1074/Jbc.271.39.23799 |
0.448 |
|
| 1995 |
Bagley KA, Duin EC, Roseboom W, Albracht SP, Woodruff WH. Infrared-detectable groups sense changes in charge density on the nickel center in hydrogenase from Chromatium vinosum. Biochemistry. 34: 5527-35. PMID 7727413 DOI: 10.1021/Bi00016A026 |
0.36 |
|
| 1994 |
Surerus KK, Chen M, van der Zwaan JW, Rusnak FM, Kolk M, Duin EC, Albracht SP, Münck E. Further characterization of the spin coupling observed in oxidized hydrogenase from Chromatium vinosum. A Mössbauer and multifrequency EPR study. Biochemistry. 33: 4980-93. PMID 8161560 DOI: 10.1021/Bi00182A029 |
0.499 |
|
| 1993 |
Surerus K, Chen M, van der Zwaan W, Kolk M, Duin E, Albracht S, Münck E. Mössbauer and EPR studies of chromatium vinosum hydrogenase Journal of Inorganic Biochemistry. 51: 448. DOI: 10.1016/0162-0134(93)85476-O |
0.336 |
|
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