| Year |
Citation |
Score |
| 2016 |
Rabus R, Boll M, Heider J, Meckenstock RU, Buckel W, Einsle O, Ermler U, Golding BT, Gunsalus RP, Kroneck PM, Krüger M, Lueders T, Martins BM, Musat F, Richnow HH, et al. Anaerobic Microbial Degradation of Hydrocarbons: From Enzymatic Reactions to the Environment. Journal of Molecular Microbiology and Biotechnology. 26: 5-28. PMID 26960061 DOI: 10.1159/000443997 |
0.564 |
|
| 2016 |
Boll M, Einsle O, Ermler U, Kroneck PM, Ullmann GM. Structure and Function of the Unusual Tungsten Enzymes Acetylene Hydratase and Class II Benzoyl-Coenzyme A Reductase. Journal of Molecular Microbiology and Biotechnology. 26: 119-37. PMID 26959374 DOI: 10.1159/000440805 |
0.577 |
|
| 2016 |
Kroneck PM. Acetylene hydratase: a non-redox enzyme with tungsten and iron-sulfur centers at the active site. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 21: 29-38. PMID 26790879 DOI: 10.1007/s00775-015-1330-y |
0.336 |
|
| 2014 |
Loschonsky S, Waltzer S, Fraas S, Wacker T, Andrade SL, Kroneck PM, Müller M. Catalytic scope of the thiamine-dependent multifunctional enzyme cyclohexane-1,2-dione hydrolase. Chembiochem : a European Journal of Chemical Biology. 15: 389-92. PMID 24436243 DOI: 10.1002/cbic.201300673 |
0.335 |
|
| 2012 |
Wüst A, Schneider L, Pomowski A, Zumft WG, Kroneck PM, Einsle O. Nature's way of handling a greenhouse gas: the copper-sulfur cluster of purple nitrous oxide reductase. Biological Chemistry. 393: 1067-77. PMID 23096349 DOI: 10.1515/Hsz-2012-0177 |
0.587 |
|
| 2012 |
Steinbach A, Fraas S, Harder J, Warkentin E, Kroneck PM, Ermler U. Crystal structure of a ring-cleaving cyclohexane-1,2-dione hydrolase, a novel member of the thiamine diphosphate enzyme family. The Febs Journal. 279: 1209-19. PMID 22309255 DOI: 10.1111/j.1742-4658.2012.08513.x |
0.373 |
|
| 2012 |
Gómez-Manzo S, González-Valdez AA, Oria-Hernández J, Reyes-Vivas H, Arreguín-Espinosa R, Kroneck PM, Sosa-Torres ME, Escamilla JE. The active (ADHa) and inactive (ADHi) forms of the PQQ-alcohol dehydrogenase from Gluconacetobacter diazotrophicus differ in their respective oligomeric structures and redox state of their corresponding prosthetic groups. Fems Microbiology Letters. 328: 106-13. PMID 22188488 DOI: 10.1111/j.1574-6968.2011.02487.x |
0.347 |
|
| 2011 |
Steinbach AK, Fraas S, Harder J, Tabbert A, Brinkmann H, Meyer A, Ermler U, Kroneck PM. Cyclohexane-1,2-dione hydrolase from denitrifying Azoarcus sp. strain 22Lin, a novel member of the thiamine diphosphate enzyme family. Journal of Bacteriology. 193: 6760-9. PMID 21965568 DOI: 10.1128/Jb.05348-11 |
0.365 |
|
| 2011 |
Pomowski A, Zumft WG, Kroneck PM, Einsle O. N2O binding at a [4Cu:2S] copper-sulphur cluster in nitrous oxide reductase. Nature. 477: 234-7. PMID 21841804 DOI: 10.1038/Nature10332 |
0.573 |
|
| 2011 |
Tenbrink F, Schink B, Kroneck PM. Exploring the active site of the tungsten, iron-sulfur enzyme acetylene hydratase. Journal of Bacteriology. 193: 1229-36. PMID 21193613 DOI: 10.1128/Jb.01057-10 |
0.335 |
|
| 2010 |
Pomowski A, Zumft WG, Kroneck PM, Einsle O. Crystallization of purple nitrous oxide reductase from Pseudomonas stutzeri. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications. 66: 1541-3. PMID 21045317 DOI: 10.1107/S1744309110038832 |
0.531 |
|
| 2010 |
Parey K, Warkentin E, Kroneck PM, Ermler U. Reaction cycle of the dissimilatory sulfite reductase from Archaeoglobus fulgidus. Biochemistry. 49: 8912-21. PMID 20822098 DOI: 10.1021/bi100781f |
0.359 |
|
| 2009 |
Fraas S, Steinbach AK, Tabbert A, Harder J, Ermler U, Tittmann K, Meyer A, Kroneck PM. Cyclohexane-1,2-dione hydrolase: A new tool to degrade alicyclic compounds Journal of Molecular Catalysis B: Enzymatic. 61: 47-49. DOI: 10.1016/J.Molcatb.2009.03.021 |
0.378 |
|
| 2008 |
Lukat P, Rudolf M, Stach P, Messerschmidt A, Kroneck PM, Simon J, Einsle O. Binding and reduction of sulfite by cytochrome c nitrite reductase. Biochemistry. 47: 2080-6. PMID 18201106 DOI: 10.1021/Bi7021415 |
0.61 |
|
| 2007 |
Seiffert GB, Ullmann GM, Messerschmidt A, Schink B, Kroneck PM, Einsle O. Structure of the non-redox-active tungsten/[4Fe:4S] enzyme acetylene hydratase. Proceedings of the National Academy of Sciences of the United States of America. 104: 3073-7. PMID 17360611 DOI: 10.1073/Pnas.0610407104 |
0.626 |
|
| 2007 |
Zumft WG, Kroneck PM. Respiratory transformation of nitrous oxide (N2O) to dinitrogen by Bacteria and Archaea. Advances in Microbial Physiology. 52: 107-227. PMID 17027372 DOI: 10.1016/S0065-2911(06)52003-X |
0.332 |
|
| 2005 |
Boll M, Schink B, Messerschmidt A, Kroneck PM. Novel bacterial molybdenum and tungsten enzymes: three-dimensional structure, spectroscopy, and reaction mechanism. Biological Chemistry. 386: 999-1006. PMID 16218872 DOI: 10.1515/Bc.2005.116 |
0.339 |
|
| 2005 |
Wunsch P, Körner H, Neese F, van Spanning RJ, Kroneck PM, Zumft WG. NosX function connects to nitrous oxide (N2O) reduction by affecting the Cu(Z) center of NosZ and its activity in vivo. Febs Letters. 579: 4605-9. PMID 16087179 DOI: 10.1016/J.Febslet.2005.07.023 |
0.471 |
|
| 2004 |
Einsle O, Kroneck PM. Structural basis of denitrification. Biological Chemistry. 385: 875-83. PMID 15551861 DOI: 10.1515/Bc.2004.115 |
0.586 |
|
| 2004 |
Messerschmidt A, Niessen H, Abt D, Einsle O, Schink B, Kroneck PM. Crystal structure of pyrogallol-phloroglucinol transhydroxylase, an Mo enzyme capable of intermolecular hydroxyl transfer between phenols. Proceedings of the National Academy of Sciences of the United States of America. 101: 11571-6. PMID 15284442 DOI: 10.1073/Pnas.0404378101 |
0.59 |
|
| 2004 |
Simon J, Einsle O, Kroneck PM, Zumft WG. The unprecedented nos gene cluster of Wolinella succinogenes encodes a novel respiratory electron transfer pathway to cytochrome c nitrous oxide reductase. Febs Letters. 569: 7-12. PMID 15225600 DOI: 10.1016/J.Febslet.2004.05.060 |
0.563 |
|
| 2002 |
Einsle O, Messerschmidt A, Huber R, Kroneck PM, Neese F. Mechanism of the six-electron reduction of nitrite to ammonia by cytochrome c nitrite reductase. Journal of the American Chemical Society. 124: 11737-45. PMID 12296741 DOI: 10.1021/Ja0206487 |
0.661 |
|
| 2002 |
Epel B, Slutter CS, Neese F, Kroneck PM, Zumft WG, Pecht I, Farver O, Lu Y, Goldfarb D. Electron-mediating Cu(A) centers in proteins: a comparative high field (1)H ENDOR study. Journal of the American Chemical Society. 124: 8152-62. PMID 12095361 DOI: 10.1021/Ja012514J |
0.445 |
|
| 2002 |
Fritz G, Büchert T, Kroneck PM. The function of the [4Fe-4S] clusters and FAD in bacterial and archaeal adenylylsulfate reductases. Evidence for flavin-catalyzed reduction of adenosine 5'-phosphosulfate. The Journal of Biological Chemistry. 277: 26066-73. PMID 12006599 DOI: 10.1074/jbc.M203397200 |
0.328 |
|
| 2002 |
Abt DJ, Einsle O, Niessen H, Krieger R, Messerschmidt A, Schink B, Kroneck PM. Crystallization and preliminary X-ray analysis of the molybdenum-dependent pyrogallol-phloroglucinol transhydroxylase of Pelobacter acidigallici. Acta Crystallographica. Section D, Biological Crystallography. 58: 343-5. PMID 11807272 DOI: 10.1107/S0907444901020443 |
0.523 |
|
| 2002 |
Einsle O, Stach P, Messerschmidt A, Klimmek O, Simon J, Kröger A, Kroneck PM. Crystallization and preliminary X-ray analysis of the membrane-bound cytochrome c nitrite reductase complex (NrfHA) from Wolinella succinogenes. Acta Crystallographica. Section D, Biological Crystallography. 58: 341-2. PMID 11807271 DOI: 10.1107/S090744490102039X |
0.572 |
|
| 2001 |
Einsle O, Foerster S, Mann K, Fritz G, Messerschmidt A, Kroneck PM. Spectroscopic investigation and determination of reactivity and structure of the tetraheme cytochrome c3 from Desulfovibrio desulfuricans Essex 6. European Journal of Biochemistry / Febs. 268: 3028-35. PMID 11358521 DOI: 10.1046/J.1432-1327.2001.02195.X |
0.57 |
|
| 2001 |
Einsle O, Stach P, Messerschmidt A, Simon J, Kröger A, Huber R, Kroneck PM. Cytochrome c nitrite reductase from Wolinella succinogenes. Structure at 1.6 A resolution, inhibitor binding, and heme-packing motifs. The Journal of Biological Chemistry. 275: 39608-16. PMID 10984487 DOI: 10.1074/Jbc.M006188200 |
0.662 |
|
| 2000 |
Stach P, Einsle O, Schumacher W, Kurun E, Kroneck PM. Bacterial cytochrome c nitrite reductase: new structural and functional aspects. Journal of Inorganic Biochemistry. 79: 381-5. PMID 10830892 DOI: 10.1016/S0162-0134(99)00248-2 |
0.619 |
|
| 2000 |
Charnock JM, Dreusch A, Körner H, Neese F, Nelson J, Kannt A, Michel H, Garner CD, Kroneck PM, Zumft WG. Structural investigations of the CuA centre of nitrous oxide reductase from Pseudomonas stutzeri by site-directed mutagenesis and X-ray absorption spectroscopy. European Journal of Biochemistry / Febs. 267: 1368-81. PMID 10691974 DOI: 10.1046/J.1432-1327.2000.01131.X |
0.481 |
|
| 2000 |
Simon J, Gross R, Einsle O, Kroneck PM, Kröger A, Klimmek O. A NapC/NirT-type cytochrome c (NrfH) is the mediator between the quinone pool and the cytochrome c nitrite reductase of Wolinella succinogenes. Molecular Microbiology. 35: 686-96. PMID 10672190 DOI: 10.1046/J.1365-2958.2000.01742.X |
0.572 |
|
| 1999 |
Meckenstock RU, Krieger R, Ensign S, Kroneck PM, Schink B. Acetylene hydratase of Pelobacter acetylenicus. Molecular and spectroscopic properties of the tungsten iron-sulfur enzyme. European Journal of Biochemistry. 264: 176-82. PMID 10447686 DOI: 10.1046/J.1432-1327.1999.00600.X |
0.315 |
|
| 1999 |
Einsle O, Messerschmidt A, Stach P, Bourenkov GP, Bartunik HD, Huber R, Kroneck PM. Structure of cytochrome c nitrite reductase. Nature. 400: 476-80. PMID 10440380 DOI: 10.1038/22802 |
0.659 |
|
| 1998 |
Kisker C, Schindelin H, Baas D, Rétey J, Meckenstock RU, Kroneck PM. A structural comparison of molybdenum cofactor-containing enzymes. Fems Microbiology Reviews. 22: 503-21. PMID 9990727 DOI: 10.1111/J.1574-6976.1998.Tb00384.X |
0.303 |
|
| 1997 |
Neese F, Zumft W, Antholine W, Kroneck P. Novel binuclear copper chromophores in biology: The CuA and Cuz sites in bacterial nitrous oxide reductase Journal of Inorganic Biochemistry. 67: 425. DOI: 10.1016/S0162-0134(97)80287-5 |
0.447 |
|
| 1996 |
Dreusch A, Riester J, Kroneck PM, Zumft WG. Mutation of the conserved Cys165 outside of the CuA domain destabilizes nitrous oxide reductase but maintains its catalytic activity. Evidence for disulfide bridges and a putative protein disulfide isomerase gene. European Journal of Biochemistry. 237: 447-53. PMID 8647084 DOI: 10.1111/J.1432-1033.1996.0447K.X |
0.321 |
|
| 1996 |
Hole UH, Vollack KU, Zumft WG, Eisenmann E, Siddiqui RA, Friedrich B, Kroneck PM. Characterization of the membranous denitrification enzymes nitrite reductase (cytochrome cd1) and copper-containing nitrous oxide reductase from Thiobacillus denitrificans. Archives of Microbiology. 165: 55-61. PMID 8639023 DOI: 10.1007/S002030050296 |
0.312 |
|
| 1995 |
Schumacher W, Hole U, Kroneck PM. Ammonia-forming cytochrome c nitrite reductase from Sulfurospirillum deleyianum is a tetraheme protein: new aspects of the molecular composition and spectroscopic properties. Biochemical and Biophysical Research Communications. 205: 911-6. PMID 7999130 DOI: 10.1006/BBRC.1994.2751 |
0.332 |
|
| 1995 |
Neese F, Zumft W, Antholine W, Kroneck P. On the nature of the CuA-site in nitrous oxide reductase from Pseudomonas stutzeri Journal of Inorganic Biochemistry. 59: 688. DOI: 10.1016/0162-0134(95)97776-M |
0.405 |
|
| 1994 |
Kastrau DH, Heiss B, Kroneck PM, Zumft WG. Nitric oxide reductase from Pseudomonas stutzeri, a novel cytochrome bc complex. Phospholipid requirement, electron paramagnetic resonance and redox properties. European Journal of Biochemistry / Febs. 222: 293-303. PMID 8020468 DOI: 10.1111/j.1432-1033.1994.tb18868.x |
0.311 |
|
| 1993 |
Antholine W, Kroneck P, Neese F, Koteich H. Analysis of EPR parameters from nitrous oxide reductase and cytochrome c oxidase Journal of Inorganic Biochemistry. 51: 360. DOI: 10.1016/0162-0134(93)85391-K |
0.432 |
|
| 1992 |
Messerschmidt A, Steigemann W, Huber R, Lang G, Kroneck PM. X-ray crystallographic characterisation of type-2-depleted ascorbate oxidase from zucchini. European Journal of Biochemistry. 209: 597-602. PMID 1330552 DOI: 10.1111/J.1432-1033.1992.Tb17325.X |
0.408 |
|
| 1991 |
Kroneck PM, Riester J, Zumft WG, Antholine WE. The copper site in nitrous oxide reductase. Biology of Metals. 3: 103-9. PMID 1965779 DOI: 10.1007/BF01179514 |
0.352 |
|
| 1991 |
Messerschmidt A, Huber R, Kroneck P. X-ray crystallographic characterisation of type-2 depleted ascorbate oxidase from zucchini Journal of Inorganic Biochemistry. 43: 189. DOI: 10.1016/0162-0134(91)84181-8 |
0.307 |
|
| 1989 |
Riester J, Zumft WG, Kroneck PM. Nitrous oxide reductase from Pseudomonas stutzeri. Redox properties and spectroscopic characterization of different forms of the multicopper enzyme. European Journal of Biochemistry. 178: 751-62. PMID 2536326 DOI: 10.1111/J.1432-1033.1989.TB14506.X |
0.314 |
|
| 1987 |
Zumft WG, Gotzmann DJ, Kroneck PM. Type 1, blue copper proteins constitute a respiratory nitrite-reducing system in Pseudomonas aureofaciens. European Journal of Biochemistry. 168: 301-7. PMID 3665926 DOI: 10.1111/J.1432-1033.1987.TB13421.X |
0.319 |
|
| 1985 |
Coyle CL, Zumft WG, Kroneck PM, Körner H, Jakob W. Nitrous oxide reductase from denitrifying Pseudomonas perfectomarina. Purification and properties of a novel multicopper enzyme. European Journal of Biochemistry / Febs. 153: 459-67. PMID 3000778 DOI: 10.1111/J.1432-1033.1985.TB09324.X |
0.367 |
|
| 1980 |
Gutman M, Bonomi F, Pagani S, Cerletti P, Kroneck P. Modulation of the flavin redox potential as mode of regulation of succinate dehydrogenase activity. Biochimica Et Biophysica Acta. 591: 400-408. PMID 7397131 DOI: 10.1016/0005-2728(80)90171-1 |
0.37 |
|
| 1980 |
Kroneck PM, Vortisch V, Hemmerich P. Model studies on the coordination of copper in biological systems. The deprotonated peptide nitrogen as a potential binding site for copper(II). European Journal of Biochemistry / Febs. 109: 603-12. PMID 6250848 DOI: 10.1111/J.1432-1033.1980.TB04833.X |
0.529 |
|
| 1980 |
Bohner H, Merkle H, Kroneck P, Boger P. High Variability of the Electron Carrier Plastocyanin in Microalgae Febs Journal. 105: 603-609. PMID 6245887 DOI: 10.1111/J.1432-1033.1980.Tb04538.X |
0.345 |
|
| 1980 |
Spence JT, Minelli M, Kroneck P. Monomeric molybdenum oxo complexes with tetradentate aromatic aminothiols. Model redox systems for molybdenum enzymes Journal of the American Chemical Society. 102: 4538-4541. DOI: 10.1021/Ja00533A050 |
0.345 |
|
| 1976 |
Siegelman MH, Rasched IR, Kunert K, Kroneck P, Böger P. Plastocyanin : Possible Significance of Quaternary Structure Febs Journal. 64: 131-140. PMID 179807 DOI: 10.1111/J.1432-1033.1976.Tb10281.X |
0.366 |
|
| 1976 |
Vortisch V, Kroneck P, Hemmerich P. Model studies on the coordination of copper in enzymes. IV. Structure and stability of cuprous complexes with sulfur-containing ligands Journal of the American Chemical Society. 98: 2821-2826. DOI: 10.1021/Ja00426A025 |
0.38 |
|
| 1971 |
Kroneck P, Naumann C, Hemmerich P. Formation and properties of binuclear cupric mercaptide five-membered chelates Inorganic and Nuclear Chemistry Letters. 7: 659-666. DOI: 10.1016/0020-1650(71)80052-1 |
0.457 |
|
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