| Year |
Citation |
Score |
| 2019 |
Hagen WR. EPR spectroscopy of putative enzyme intermediates in the NO reductase and the auto-nitrosylation reaction of Desulfovibrio vulgaris hybrid cluster protein. Febs Letters. PMID 31318443 DOI: 10.1002/1873-3468.13539 |
0.318 |
|
| 2018 |
Hagen WR. EPR spectroscopy of complex biological iron-sulfur systems. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. PMID 29468426 DOI: 10.1007/s00775-018-1543-y |
0.363 |
|
| 2017 |
Mitić S, Strampraad MJF, Hagen WR, de Vries S. Microsecond time-scale kinetics of transient biochemical reactions. Plos One. 12: e0185888. PMID 28973014 DOI: 10.1371/journal.pone.0185888 |
0.491 |
|
| 2017 |
Hagen WR, Hagedoorn PL, Honarmand Ebrahimi K. The workings of ferritin: a crossroad of opinions. Metallomics : Integrated Biometal Science. PMID 28573266 DOI: 10.1039/c7mt00124j |
0.34 |
|
| 2017 |
Ebrahimi KH, Bill E, Hagedoorn PL, Hagen WR. Spectroscopic evidence for the presence of a high-valent Fe(IV) species in the ferroxidase reaction of an archaeal ferritin. Febs Letters. PMID 28542723 DOI: 10.1002/1873-3468.12697 |
0.335 |
|
| 2016 |
Ebrahimi KH, Bill E, Hagedoorn PL, Hagen WR. Spectroscopic evidence for the role of a site of the di-iron catalytic center of ferritins in tuning the kinetics of Fe(ii) oxidation. Molecular Biosystems. PMID 27722502 DOI: 10.1039/c6mb00235h |
0.314 |
|
| 2015 |
Honarmand Ebrahimi K, Hagedoorn PL, Hagen WR. Unity in the biochemistry of the iron-storage proteins ferritin and bacterioferritin. Chemical Reviews. 115: 295-326. PMID 25418839 DOI: 10.1021/cr5004908 |
0.309 |
|
| 2013 |
Ebrahimi KH, Hagedoorn PL, Hagen WR. A conserved tyrosine in ferritin is a molecular capacitor. Chembiochem : a European Journal of Chemical Biology. 14: 1123-33. PMID 23737293 DOI: 10.1002/cbic.201300149 |
0.303 |
|
| 2013 |
van Vugt-Lussenburg BM, van der Weel L, Hagen WR, Hagedoorn PL. Biochemical similarities and differences between the catalytic [4Fe-4S] cluster containing fumarases FumA and FumB from Escherichia coli. Plos One. 8: e55549. PMID 23405168 DOI: 10.1371/journal.pone.0055549 |
0.356 |
|
| 2013 |
Martic M, Jakab-Simon IN, Haahr LT, Hagen WR, Christensen HE. Heterometallic [AgFe(3)S (4)] ferredoxin variants: synthesis, characterization, and the first crystal structure of an engineered heterometallic iron-sulfur protein. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 18: 261-76. PMID 23296387 DOI: 10.1007/s00775-012-0971-3 |
0.382 |
|
| 2013 |
Honarmand Ebrahimi K, Hagedoorn PL, Hagen WR. Phosphate accelerates displacement of Fe(III) by Fe(II) in the ferroxidase center of Pyrococcus furiosus ferritin. Febs Letters. 587: 220-5. PMID 23247211 DOI: 10.1016/j.febslet.2012.11.029 |
0.31 |
|
| 2013 |
Ebrahimi KH, Bill E, Hagedoorn P, Hagen WR. Erratum: Corrigendum: The catalytic center of ferritin regulates iron storage via Fe(II)-Fe(III) displacement Nature Chemical Biology. 9: 406-406. DOI: 10.1038/nchembio0613-406c |
0.313 |
|
| 2012 |
Honarmand Ebrahimi K, Bill E, Hagedoorn PL, Hagen WR. The catalytic center of ferritin regulates iron storage via Fe(II)-Fe(III) displacement. Nature Chemical Biology. 8: 941-8. PMID 23001032 DOI: 10.1038/nchembio.1071 |
0.343 |
|
| 2012 |
Ebrahimi KH, Hagedoorn PL, Hagen WR. A synthetic peptide with the putative iron binding motif of amyloid precursor protein (APP) does not catalytically oxidize iron. Plos One. 7: e40287. PMID 22916096 DOI: 10.1371/journal.pone.0040287 |
0.307 |
|
| 2012 |
Ebrahimi KH, Hagedoorn PL, van der Weel L, Verhaert PD, Hagen WR. A novel mechanism of iron-core formation by Pyrococcus furiosus archaeoferritin, a member of an uncharacterized branch of the ferritin-like superfamily. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 17: 975-85. PMID 22739810 DOI: 10.1007/s00775-012-0913-0 |
0.338 |
|
| 2011 |
Sevcenco AM, Pinkse MW, Wolterbeek HT, Verhaert PD, Hagen WR, Hagedoorn PL. Exploring the microbial metalloproteome using MIRAGE. Metallomics : Integrated Biometal Science. 3: 1324-30. PMID 22094925 DOI: 10.1039/c1mt00154j |
0.347 |
|
| 2010 |
Honarmand Ebrahimi K, Hagedoorn PL, Hagen WR. Inhibition and stimulation of formation of the ferroxidase center and the iron core in Pyrococcus furiosus ferritin. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 15: 1243-53. PMID 20582559 DOI: 10.1007/s00775-010-0682-6 |
0.322 |
|
| 2009 |
Honarmand Ebrahimi K, Hagedoorn PL, Jongejan JA, Hagen WR. Catalysis of iron core formation in Pyrococcus furiosus ferritin. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 14: 1265-74. PMID 19623480 DOI: 10.1007/s00775-009-0571-z |
0.334 |
|
| 2009 |
van Vugt-Lussenburg BM, van der Weel L, Hagen WR, Hagedoorn PL. Identification of two [4Fe-4S]-cluster-containing hydro-lyases from Pyrococcus furiosus. Microbiology (Reading, England). 155: 3015-20. PMID 19520720 DOI: 10.1099/mic.0.030320-0 |
0.374 |
|
| 2009 |
Overeijnder ML, Hagen WR, Hagedoorn PL. A thermostable hybrid cluster protein from Pyrococcus furiosus: effects of the loss of a three helix bundle subdomain. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 14: 703-10. PMID 19241093 DOI: 10.1007/s00775-009-0483-y |
0.344 |
|
| 2008 |
Heering HA, Bulsink YBM, Hagen WR, Meyer TE. Reversible Super-Reduction of the Cubane [4Fe-4S](3+;2+;1+) in the High-Potential Iron-Sulfur Protein Under Non-Denaturing Conditions European Journal of Biochemistry. 232: 811-817. DOI: 10.1111/j.1432-1033.1995.0811a.x |
0.381 |
|
| 2006 |
Bol E, Bevers LE, Hagedoorn PL, Hagen WR. Redox chemistry of tungsten and iron-sulfur prosthetic groups in Pyrococcus furiosus formaldehyde ferredoxin oxidoreductase. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 11: 999-1006. PMID 16924554 DOI: 10.1007/s00775-006-0155-0 |
0.366 |
|
| 2006 |
Hasan MN, Kwakernaak C, Sloof WG, Hagen WR, Heering HA. Pyrococcus furiosus 4Fe-ferredoxin, chemisorbed on gold, exhibits gated reduction and ionic strength dependent dimerization. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 11: 651-62. PMID 16791647 DOI: 10.1007/s00775-006-0117-6 |
0.334 |
|
| 2006 |
Carette N, Hagen W, Bertrand L, de Val N, Vertommen D, Roland F, Hue L, Crichton RR. Optical and EPR spectroscopic studies of demetallation of hemin by L-chain apoferritins Journal of Inorganic Biochemistry. 100: 1426-1435. PMID 16781777 DOI: 10.1016/J.Jinorgbio.2006.03.015 |
0.5 |
|
| 2006 |
Tatur J, Hagedoorn PL, Overeijnder ML, Hagen WR. A highly thermostable ferritin from the hyperthermophilic archaeal anaerobe Pyrococcus furiosus. Extremophiles : Life Under Extreme Conditions. 10: 139-48. PMID 16341820 DOI: 10.1007/s00792-005-0484-x |
0.362 |
|
| 2005 |
Bevers LE, Bol E, Hagedoorn PL, Hagen WR. WOR5, a novel tungsten-containing aldehyde oxidoreductase from Pyrococcus furiosus with a broad substrate Specificity. Journal of Bacteriology. 187: 7056-61. PMID 16199576 DOI: 10.1128/JB.187.20.7056-7061.2005 |
0.334 |
|
| 2005 |
Tatur J, Hagen WR. The dinuclear iron-oxo ferroxidase center of Pyrococcus furiosus ferritin is a stable prosthetic group with unexpectedly high reduction potentials. Febs Letters. 579: 4729-32. PMID 16107254 DOI: 10.1016/j.febslet.2005.07.045 |
0.39 |
|
| 2005 |
Priem AH, Klaassen AA, Reijerse EJ, Meyer TE, Luchinat C, Capozzi F, Dunham WR, Hagen WR. EPR analysis of multiple forms of [4Fe-4S](3+) clusters in HiPIPs. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 10: 417-24. PMID 15889286 DOI: 10.1007/S00775-005-0656-2 |
0.408 |
|
| 2005 |
Chakraborty S, Behrens M, Herman PL, Arendsen AF, Hagen WR, Carlson DL, Wang XZ, Weeks DP. A three-component dicamba O-demethylase from Pseudomonas maltophilia, strain DI-6: purification and characterization. Archives of Biochemistry and Biophysics. 437: 20-8. PMID 15820213 DOI: 10.1016/J.Abb.2005.02.024 |
0.395 |
|
| 2005 |
Hagedoorn PL, Chen T, Schröder I, Piersma SR, de Vries S, Hagen WR. Purification and characterization of the tungsten enzyme aldehyde:ferredoxin oxidoreductase from the hyperthermophilic denitrifier Pyrobaculum aerophilum. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 10: 259-69. PMID 15772818 DOI: 10.1007/s00775-005-0637-5 |
0.614 |
|
| 2003 |
Maillard J, Schumacher W, Vazquez F, Regeard C, Hagen WR, Holliger C. Characterization of the corrinoid iron-sulfur protein tetrachloroethene reductive dehalogenase of Dehalobacter restrictus. Applied and Environmental Microbiology. 69: 4628-38. PMID 12902251 DOI: 10.1128/Aem.69.8.4628-4638.2003 |
0.352 |
|
| 2003 |
de Bok FA, Hagedoorn PL, Silva PJ, Hagen WR, Schiltz E, Fritsche K, Stams AJ. Two W-containing formate dehydrogenases (CO2-reductases) involved in syntrophic propionate oxidation by Syntrophobacter fumaroxidans. European Journal of Biochemistry / Febs. 270: 2476-85. PMID 12755703 DOI: 10.1046/j.1432-1033.2003.03619.x |
0.314 |
|
| 2002 |
Hagedoorn PL, De Geus DC, Hagen WR. Spectroscopic characterization and ligand-binding properties of chlorite dismutase from the chlorate respiring bacterial strain GR-1. European Journal of Biochemistry / Febs. 269: 4905-11. PMID 12354122 DOI: 10.1046/j.1432-1033.2002.03208.x |
0.375 |
|
| 2002 |
Macedo S, Mitchell EP, Romão CV, Cooper SJ, Coelho R, Liu MY, Xavier AV, LeGall J, Bailey S, Garner DC, Hagen WR, Teixeira M, Carrondo MA, Lindley P. Hybrid cluster proteins (HCPs) from Desulfovibrio desulfuricans ATCC 27774 and Desulfovibrio vulgaris (Hildenborough): X-ray structures at 1.25 A resolution using synchrotron radiation. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 7: 514-25. PMID 11941509 DOI: 10.1007/s00775-001-0326-y |
0.329 |
|
| 2001 |
Hagedoorn PL, Schmidt PP, Andersson KK, Hagen WR, Flatmark T, Martínez A. The effect of substrate, dihydrobiopterin, and dopamine on the EPR spectroscopic properties and the midpoint potential of the catalytic iron in recombinant human phenylalanine hydroxylase. The Journal of Biological Chemistry. 276: 22850-6. PMID 11301319 DOI: 10.1074/jbc.M009458200 |
0.347 |
|
| 2000 |
Cooper SJ, Garner CD, Hagen WR, Lindley PF, Bailey S. Hybrid-cluster protein (HCP) from Desulfovibrio vulgaris (Hildenborough) at 1.6 A resolution. Biochemistry. 39: 15044-54. PMID 11106482 DOI: 10.1021/bi001483m |
0.342 |
|
| 2000 |
Silva PJ, van den Ban EC, Wassink H, Haaker H, de Castro B, Robb FT, Hagen WR. Enzymes of hydrogen metabolism in Pyrococcus furiosus. European Journal of Biochemistry / Febs. 267: 6541-51. PMID 11054105 DOI: 10.1046/J.1432-1327.2000.01745.X |
0.444 |
|
| 2000 |
Hagen WR, Silva PJ, Amorim MA, Hagedoorn PL, Wassink H, Haaker H, Robb FT. Novel structure and redox chemistry of the prosthetic groups of the iron-sulfur flavoprotein sulfide dehydrogenase from Pyrococcus furiosus; evidence for a [2Fe-2S] cluster with Asp(Cys)3 ligands. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 5: 527-34. PMID 10968624 DOI: 10.1007/Pl00021452 |
0.432 |
|
| 2000 |
Hagen WR, Vanoni MA, Rosenbaum K, Schnackerz KD. On the iron-sulfur clusters in the complex redox enzyme dihydropyrimidine dehydrogenase. European Journal of Biochemistry / Febs. 267: 3640-6. PMID 10848981 DOI: 10.1046/j.1432-1327.2000.01393.x |
0.438 |
|
| 2000 |
van den Berg WA, Hagen WR, van Dongen WM. The hybrid-cluster protein ('prismane protein') from Escherichia coli. Characterization of the hybrid-cluster protein, redox properties of the [2Fe-2S] and [4Fe-2S-2O] clusters and identification of an associated NADH oxidoreductase containing FAD and [2Fe-2S]. European Journal of Biochemistry / Febs. 267: 666-76. PMID 10651802 DOI: 10.1046/j.1432-1327.2000.01032.x |
0.399 |
|
| 1999 |
Kengen SW, Rikken GB, Hagen WR, van Ginkel CG, Stams AJ. Purification and characterization of (per)chlorate reductase from the chlorate-respiring strain GR-1. Journal of Bacteriology. 181: 6706-11. PMID 10542172 DOI: 10.1128/jb.181.21.6706-6711.1999 |
0.382 |
|
| 1999 |
Silva PJ, de Castro B, Hagen WR. On the prosthetic groups of the NiFe sulfhydrogenase from Pyrococcus furiosus: topology, structure, and temperature-dependent redox chemistry. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 4: 284-91. PMID 10439073 DOI: 10.1007/s007750050314 |
0.315 |
|
| 1999 |
van de Pas BA, Smidt H, Hagen WR, van der Oost J, Schraa G, Stams AJ, de Vos WM. Purification and molecular characterization of ortho-chlorophenol reductive dehalogenase, a key enzyme of halorespiration in Desulfitobacterium dehalogenans. The Journal of Biological Chemistry. 274: 20287-92. PMID 10400648 DOI: 10.1074/jbc.274.29.20287 |
0.386 |
|
| 1998 |
Pierik AJ, Hulstein M, Hagen WR, Albracht SP. A low-spin iron with CN and CO as intrinsic ligands forms the core of the active site in [Fe]-hydrogenases. European Journal of Biochemistry / Febs. 258: 572-8. PMID 9874225 DOI: 10.1046/J.1432-1327.1998.2580572.X |
0.716 |
|
| 1998 |
Spee JH, Arendsen AF, Wassink H, Marritt SJ, Hagen WR, Haaker H. Redox properties and electron paramagnetic resonance spectroscopy of the transition state complex of Azotobacter vinelandii nitrogenase. Febs Letters. 432: 55-8. PMID 9710250 DOI: 10.1016/S0014-5793(98)00827-8 |
0.377 |
|
| 1998 |
Kröckel M, Trautwein AX, Arendsen AF, Hagen WR. The prismane protein resolved--Mössbauer investigation of a 4Fe cluster with an unusual mixture of bridging ligands and metal coordinations. European Journal of Biochemistry / Febs. 251: 454-61. PMID 9492318 DOI: 10.1046/j.1432-1327.1998.2510454.x |
0.433 |
|
| 1998 |
Arendsen AF, Hadden J, Card G, McAlpine AS, Bailey S, Zaitsev V, Duke EHM, Lindley PF, Kröckel M, Trautwein AX, Feiters MC, Charnock JM, Garner CD, Marritt SJ, Thomson AJ, ... ... Hagen WR, et al. The 'prismane' protein resolved: X-ray structure at 1.7 Å and multiple spectroscopy of two novel 4Fe clusters Journal of Biological Inorganic Chemistry. 3: 81-95. DOI: 10.1007/S007750050210 |
0.384 |
|
| 1998 |
Hagen WR, Van Den Berg WAM, Van Dongen WMAM, Reijerse EJ, Van Kan PJM. EPR spectroscopy of biological iron-sulfur clusters with spin-admixed S = 3/2 ground states Journal of the Chemical Society - Faraday Transactions. 94: 2969-2973. |
0.35 |
|
| 1998 |
Kröckel M, Trautwein AX, Winkler H, Arendsen AF, Hagen WR. Discovery of novel iron clusters in proteins by Mössbauer spectroscopy Hyperfine Interactions. 113: 3-14. |
0.364 |
|
| 1997 |
van Dam PJ, Reijerse EJ, Hagen WR. Identification of a putative histidine base and of a non-protein nitrogen ligand in the active site of Fe-hydrogenases by one-dimensional and two-dimensional electron spin-echo envelope-modulation spectroscopy. European Journal of Biochemistry / Febs. 248: 355-61. PMID 9346288 DOI: 10.1111/j.1432-1033.1997.00355.x |
0.316 |
|
| 1997 |
Rosenbaum K, Schaffrath B, Hagen WR, Jahnke K, Gonzalez FJ, Cook PF, Schnackerz KD. Purification, characterization, and kinetics of porcine recombinant dihydropyrimidine dehydrogenase. Protein Expression and Purification. 10: 185-91. PMID 9226714 DOI: 10.1006/Prep.1997.0735 |
0.415 |
|
| 1997 |
Schumacher W, Holliger C, Zehnder AJ, Hagen WR. Redox chemistry of cobalamin and iron-sulfur cofactors in the tetrachloroethene reductase of Dehalobacter restrictus. Febs Letters. 409: 421-5. PMID 9224702 DOI: 10.1016/S0014-5793(97)00520-6 |
0.375 |
|
| 1996 |
Eggen RI, van Kranenburg R, Vriesema AJ, Geerling AC, Verhagen MF, Hagen WR, de Vos WM. Carbon monoxide dehydrogenase from Methanosarcina frisia Gö1. Characterization of the enzyme and the regulated expression of two operon-like cdh gene clusters. The Journal of Biological Chemistry. 271: 14256-63. PMID 8662887 DOI: 10.1074/jbc.271.24.14256 |
0.401 |
|
| 1996 |
van der Spek TM, Arendsen AF, Happe RP, Yun S, Bagley KA, Stufkens DJ, Hagen WR, Albracht SP. Similarities in the architecture of the active sites of Ni-hydrogenases and Fe-hydrogenases detected by means of infrared spectroscopy. European Journal of Biochemistry / Febs. 237: 629-34. PMID 8647106 DOI: 10.1111/J.1432-1033.1996.0629P.X |
0.716 |
|
| 1996 |
Van Kuijk BL, Van Loo ND, Arendsen AF, Hagen WR, Stams AJ. Purification and characterization of fumarase from the syntrophic propionate-oxidizing bacterium strain MPOB. Archives of Microbiology. 165: 126-31. PMID 8593099 DOI: 10.1007/s002030050307 |
0.399 |
|
| 1995 |
Verhagen MF, Link TA, Hagen WR. Electrochemical study of the redox properties of [2Fe-2S] ferredoxins. Evidence for superreduction of the Rieske [2Fe-2S] cluster. Febs Letters. 361: 75-8. PMID 7890043 DOI: 10.1016/0014-5793(95)00152-Y |
0.358 |
|
| 1995 |
Teixeira M, Batista R, Campos AP, Gomes C, Mendes J, Pacheco I, Anemuller S, Hagen WR. A seven-iron ferredoxin from the thermoacidophilic archaeon Desulfurolobus ambivalens. European Journal of Biochemistry. 227: 322-7. PMID 7851403 DOI: 10.1111/J.1432-1033.1995.Tb20392.X |
0.395 |
|
| 1995 |
Daas PJ, Hagen WR, Keltjens JT, Vogels GD. Characterization and determination of the redox properties of the 2[4Fe-4S] ferredoxin from Methanosarcina barkeri strain MS. Febs Letters. 356: 342-4. PMID 7805869 DOI: 10.1016/0014-5793(94)01313-6 |
0.371 |
|
| 1995 |
Aliverti A, Hagen WR, Zanetti G. Direct electrochemistry and EPR spectroscopy of spinach ferredoxin mutants with modified electron transfer properties. Febs Letters. 368: 220-4. PMID 7628609 DOI: 10.1016/0014-5793(95)00648-S |
0.41 |
|
| 1995 |
Arendsen AF, Veenhuizen PT, Hagen WR. Redox properties of the sulfhydrogenase from Pyrococcus furiosus. Febs Letters. 368: 117-21. PMID 7615063 DOI: 10.1016/0014-5793(95)00622-G |
0.361 |
|
| 1995 |
Marritt SJ, Farrar JA, Breton JL, Hagen WR, Thomson AJ. Characterization of the prismane protein from Desulfovibrio vulgaris (Hildenborough) by low-temperature magnetic circular dichroic spectroscopy. European Journal of Biochemistry. 232: 501-5. PMID 7556199 DOI: 10.1111/J.1432-1033.1995.501Zz.X |
0.412 |
|
| 1995 |
Heering HA, Bulsink YBM, Hagen WR, Meyer TE. Reversible Super-Reduction of the Cubane [4Fe-4S](3+;2+;1+) in the High-Potential Iron-Sulfur Protein Under Non-Denaturing Conditions. EPR Spectroscopic and Electrochemical Studies European Journal of Biochemistry. 232: 811-817. DOI: 10.1111/j.1432-1033.1995.tb20877.x |
0.389 |
|
| 1994 |
Verhagen MF, Kooter IM, Wolbert RB, Hagen WR. On the iron-sulfur cluster of adenosine phosphosulfate reductase from Desulfovibrio vulgaris (Hildenborough). European Journal of Biochemistry / Febs. 221: 831-7. PMID 8174563 DOI: 10.1111/j.1432-1033.1994.tb18797.x |
0.316 |
|
| 1994 |
Dorovska-Taran V, van Hoek A, Link TA, Visser AJ, Hagen WR. A comparative picosecond-resolved fluorescence study of tryptophan residues in iron-sulfur proteins. Febs Letters. 348: 305-10. PMID 8034060 DOI: 10.1016/0014-5793(94)00606-7 |
0.349 |
|
| 1994 |
van den Berg WA, Stevens AA, Verhagen MF, van Dongen WM, Hagen WR. Overproduction of the prismane protein from Desulfovibrio desulfuricans ATCC 27774 in Desulfovibrio vulgaris (Hildenborough) and EPR spectroscopy of the [6Fe-6S] cluster in different redox states. Biochimica Et Biophysica Acta. 1206: 240-6. PMID 8003528 DOI: 10.1016/0167-4838(94)90214-3 |
0.398 |
|
| 1994 |
Hagen W. Quantitative EPR of integer spin systems in iron-sulfur proteins Journal of Inorganic Biochemistry. 56: 45. DOI: 10.1016/0162-0134(94)85085-2 |
0.323 |
|
| 1993 |
Arendsen AF, Verhagen MF, Wolbert RB, Pierik AJ, Stams AJ, Jetten MS, Hagen WR. The dissimilatory sulfite reductase from Desulfosarcina variabilis is a desulforubidin containing uncoupled metalated sirohemes and S = 9/2 iron-sulfur clusters. Biochemistry. 32: 10323-30. PMID 8399175 DOI: 10.1021/Bi00090A007 |
0.398 |
|
| 1993 |
Pierik AJ, Wassink H, Haaker H, Hagen WR. Redox properties and EPR spectroscopy of the P clusters of Azotobacter vinelandii MoFe protein. European Journal of Biochemistry. 212: 51-61. PMID 8383042 DOI: 10.1111/j.1432-1033.1993.tb17632.x |
0.304 |
|
| 1993 |
Pierik AJ, Wolbert RB, Portier GL, Verhagen MF, Hagen WR. Nigerythrin and rubrerythrin from Desulfovibrio vulgaris each contain two mononuclear iron centers and two dinuclear iron clusters. European Journal of Biochemistry / Febs. 212: 237-45. PMID 8383040 DOI: 10.1111/j.1432-1033.1993.tb17655.x |
0.401 |
|
| 1992 |
Pierik AJ, Hagen WR, Redeker JS, Wolbert RB, Boersma M, Verhagen MF, Grande HJ, Veeger C, Mutsaers PH, Sands RH. Redox properties of the iron-sulfur clusters in activated Fe-hydrogenase from Desulfovibrio vulgaris (Hildenborough). European Journal of Biochemistry / Febs. 209: 63-72. PMID 1396719 DOI: 10.1111/J.1432-1033.1992.Tb17261.X |
0.72 |
|
| 1992 |
Stokkermans JP, Pierik AJ, Wolbert RB, Hagen WR, Van Dongen WM, Veeger C. The primary structure of a protein containing a putative [6Fe-6S] prismane cluster from Desulfovibrio vulgaris (Hildenborough). European Journal of Biochemistry / Febs. 208: 435-42. PMID 1339351 DOI: 10.1111/j.1432-1033.1992.tb17205.x |
0.69 |
|
| 1992 |
Stokkermans JP, Houba PH, Pierik AJ, Hagen WR, van Dongen WM, Veeger C. Overproduction of prismane protein in Desulfovibrio vulgaris (Hildenborough): evidence for a second S = 1/2-spin system in the one-electron reduced state. European Journal of Biochemistry / Febs. 210: 983-8. PMID 1336462 DOI: 10.1111/J.1432-1033.1992.Tb17503.X |
0.71 |
|
| 1992 |
Pierik AJ, Wolbert RB, Mutsaers PH, Hagen WR, Veeger C. Purification and biochemical characterization of a putative [6Fe-6S] prismane-cluster-containing protein from Desulfovibrio vulgaris (Hildenborough). European Journal of Biochemistry / Febs. 206: 697-704. PMID 1318832 DOI: 10.1111/J.1432-1033.1992.Tb16976.X |
0.703 |
|
| 1992 |
Müller A, Schneider K, Knüttel K, Hagen WR. EPR spectroscopic characterization of an 'iron only' nitrogenase. S = 3/2 spectrum of component 1 isolated from Rhodobacter capsulatus. Febs Letters. 303: 36-40. PMID 1317300 DOI: 10.1016/0014-5793(92)80472-S |
0.36 |
|
| 1992 |
Pierik AJ, Hagen WR, Dunham WR, Sands RH. Multi-frequency EPR and high-resolution Mossbauer spectroscopy of a putative [6Fe-6S] prismane-cluster-containing protein from Desulfovibrio vulgaris (Hildenborough). Characterization of a supercluster and superspin model protein European Journal of Biochemistry. 206: 705-719. DOI: 10.1111/j.1432-1033.1992.tb16977.x |
0.381 |
|
| 1991 |
Pierik AJ, Hagen WR. S = 9/2 EPR signals are evidence against coupling between the siroheme and the Fe/S cluster prosthetic groups in Desulfovibrio vulgaris (Hildenborough) dissimilatory sulfite reductase. European Journal of Biochemistry. 195: 505-16. PMID 1847685 DOI: 10.1111/j.1432-1033.1991.tb15731.x |
0.423 |
|
| 1991 |
Jetten MS, Hagen WR, Pierik AJ, Stams AJ, Zehnder AJ. Paramagnetic centers and acetyl-coenzyme A/CO exchange activity of carbon monoxide dehydrogenase from Methanothrix soehngenii. European Journal of Biochemistry / Febs. 195: 385-91. PMID 1847679 DOI: 10.1111/J.1432-1033.1991.Tb15717.X |
0.362 |
|
| 1991 |
Dunham WR, Hagen WR, Fee JA, Sands RH, Dunbar JB, Humblet C. An investigation of Chromatium vinosum high-potential irondashsulfur protein by EPR and Mossbauer spectroscopy; evidence for a freezing-induced dimerization in NaCl solutions Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 1079: 253-262. PMID 1655037 DOI: 10.1016/0167-4838(91)90066-9 |
0.412 |
|
| 1991 |
Brons HJ, Hagen WR, Zehnder AJ. Ferrous iron dependent nitric oxide production in nitrate reducing cultures of Escherichia coli. Archives of Microbiology. 155: 341-7. PMID 1646589 DOI: 10.1007/Bf00243453 |
0.307 |
|
| 1991 |
Hagen W, Pierik A, Wolbert R, Wassink H, Haaker H, Veeger C, Jetten M, Stams A, Zehnder A. S = 9/2 EPR of iron-sulfur clusters in the prismane protein, sulfite reductase, CO dehydrogenase, and nitrogenase Journal of Inorganic Biochemistry. 43: 237. DOI: 10.1016/0162-0134(91)84227-Z |
0.693 |
|
| 1989 |
Filipiak M, Hagen WR, Veeger C. Hydrodynamic, structural and magnetic properties of Megasphaera elsdenii Fe hydrogenase reinvestigated. European Journal of Biochemistry / Febs. 185: 547-53. PMID 2556270 DOI: 10.1111/J.1432-1033.1989.Tb15148.X |
0.718 |
|
| 1989 |
Hagen WR, Pierik AJ, Veeger C. Novel electron paramagnetic resonance signals from an Fe/S protein containing six iron atoms Journal of the Chemical Society, Faraday Transactions 1: Physical Chemistry in Condensed Phases. 85: 4083-4090. DOI: 10.1039/F19898504083 |
0.691 |
|
| 1988 |
Hagen WR, Wassink H, Eady RR, Smith BE, Haaker H. Quantitative EPR of an S = 7/2 system in thionine-oxidized MoFe proteins of nitrogenase. A redefinition of the P-cluster concept. European Journal of Biochemistry. 169: 457-65. PMID 2826146 DOI: 10.1111/j.1432-1033.1987.tb13633.x |
0.334 |
|
| 1988 |
Dongen W, Hagen W, Berg W, Veeger C. Evidence for an unusual mechanism of membrane translocation of the periplasmic hydrogenase ofDesulfovibrio vulgaris(Hildenborough), as derived from expression inEscherichia coli Fems Microbiology Letters. 50: 5-9. DOI: 10.1111/j.1574-6968.1988.tb02902.x |
0.594 |
|
| 1988 |
van Dongen W, Hagen W, van den Berg W, Veeger C. Evidence for an unusual mechanism of membrane translocation of the periplasmic hydrogenase of Desulfovibrio vulgaris (Hildenborough), as derived from expression in Escherichia coli Fems Microbiology Letters. 50: 5-9. DOI: 10.1111/J.1574-6968.1988.Tb02902.X |
0.642 |
|
| 1987 |
Voordouw G, Hagen WR, Krüse-Wolters KM, van Berkel-Arts A, Veeger C. Purification and characterization of Desulfovibrio vulgaris (Hildenborough) hydrogenase expressed in Escherichia coli. European Journal of Biochemistry / Febs. 162: 31-6. PMID 3028789 DOI: 10.1111/J.1432-1033.1987.Tb10537.X |
0.696 |
|
| 1986 |
van Berkel-Arts A, Dekker M, van Dijk C, Grande HJ, Hagen WR, Hilhorst R, Krüse-Wolters M, Laane C, Veeger C. Application of hydrogenase in biotechnological conversions. Biochimie. 68: 201-9. PMID 3015246 DOI: 10.1016/S0300-9084(86)81084-7 |
0.604 |
|
| 1986 |
Hagen WR, van Berkel-Arts A, Krüse-Wolters KM, Dunham WR, Veeger C. EPR of a novel high-spin component in activated hydrogenase from Desulfovibrio vulgaris (Hildenborough). Febs Letters. 201: 158-62. PMID 3011503 DOI: 10.1016/0014-5793(86)80590-7 |
0.642 |
|
| 1986 |
Hagen WR, van Berkel-Arts A, Krüse-Wolters KM, Voordouw G, Veeger C. The iron-sulfur composition of the active site of hydrogenase from Desulfovibrio vulgaris (Hildenborough) deduced from its subunit structure and total iron-sulfur content Febs Letters. 203: 59-63. DOI: 10.1016/0014-5793(86)81436-3 |
0.71 |
|
| 1985 |
Dunham WR, Hagen WR, Braaksma A, Grande HJ, Haaker H. The importance of quantitative Mössbauer spectroscopy of MoFe-protein from Azotobacter vinelandii. European Journal of Biochemistry / Febs. 146: 497-501. PMID 3855748 DOI: 10.1111/J.1432-1033.1985.Tb08679.X |
0.366 |
|
| 1985 |
Hagen WR, Dunham WR, Braaksma A, Haaker H. On the prosthetic group(s) of component II from nitrogenase. EPR of the Fe-protein from Azotobacter vinelandii. Febs Letters. 187: 146-50. PMID 2991004 DOI: 10.1016/0014-5793(85)81231-X |
0.431 |
|
| 1985 |
Hagen WR, Dunham WR, Johnson MK, Fee JA. Quarter field resonance and integer-spin/half-spin interaction in the EPR of Thermus thermophilus ferredoxin. Possible new fingerprints for three iron clusters. Biochimica Et Biophysica Acta. 828: 369-74. PMID 2985120 DOI: 10.1016/0167-4838(85)90318-8 |
0.414 |
|
| 1982 |
Hagen WR, Albracht SP. Analysis of strain-induced EPR-line shapes and anisotropic spin-lattice relaxation in a [2Fe-2S] ferredoxin. Biochimica Et Biophysica Acta. 702: 61-71. PMID 6279164 DOI: 10.1016/0167-4838(82)90027-9 |
0.676 |
|
| 1980 |
Albracht SP, van Verseveld HW, Hagen WR, Kalkman ML. A comparison of the respiratory chain in particles from Paracoccus denitrificans and bovine heart mitochondria by EPR spectroscopy. Biochimica Et Biophysica Acta. 593: 173-86. PMID 6263319 DOI: 10.1016/0005-2728(80)90055-9 |
0.622 |
|
| Show low-probability matches. |