Simon P.J. Albracht - Publications

Affiliations: 
University of Amsterdam, Amsterdam, Netherlands 

80 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2010 Albracht SP. The reaction of NADPH with bovine mitochondrial NADH:ubiquinone oxidoreductase revisited: II. Comparison of the proposed working hypothesis with literature data. Journal of Bioenergetics and Biomembranes. 42: 279-92. PMID 20632077 DOI: 10.1007/S10863-010-9302-Y  0.417
2009 Silakov A, Wenk B, Reijerse E, Albracht SP, Lubitz W. Spin distribution of the H-cluster in the H(ox)-CO state of the [FeFe] hydrogenase from Desulfovibrio desulfuricans: HYSCORE and ENDOR study of (14)N and (13)C nuclear interactions. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 14: 301-13. PMID 19011912 DOI: 10.1007/S00775-008-0449-5  0.395
2008 Hoeben FJ, Meijer FS, Dekker C, Albracht SP, Heering HA, Lemay SG. Toward single-enzyme molecule electrochemistry: [NiFe]-hydrogenase protein film voltammetry at nanoelectrodes. Acs Nano. 2: 2497-504. PMID 19206284 DOI: 10.1021/Nn800518D  0.307
2007 Silakov A, Reijerse EJ, Albracht SP, Hatchikian EC, Lubitz W. The electronic structure of the H-cluster in the [FeFe]-hydrogenase from Desulfovibrio desulfuricans: a Q-band 57Fe-ENDOR and HYSCORE study. Journal of the American Chemical Society. 129: 11447-58. PMID 17722921 DOI: 10.1021/Ja072592S  0.392
2007 Schröder O, Bleijlevens B, de Jongh TE, Chen Z, Li T, Fischer J, Förster J, Friedrich CG, Bagley KA, Albracht SP, Lubitz W. Characterization of a cyanobacterial-like uptake [NiFe] hydrogenase: EPR and FTIR spectroscopic studies of the enzyme from Acidithiobacillus ferrooxidans. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 12: 212-33. PMID 17082918 DOI: 10.1007/S00775-006-0185-7  0.387
2007 Long M, Liu J, Chen Z, Bleijlevens B, Roseboom W, Albracht SP. Characterization of a HoxEFUYH type of [NiFe] hydrogenase from Allochromatium vinosum and some EPR and IR properties of the hydrogenase module. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 12: 62-78. PMID 16969669 DOI: 10.1007/S00775-006-0162-1  0.405
2006 van der Linden E, Burgdorf T, de Lacey AL, Buhrke T, Scholte M, Fernandez VM, Friedrich B, Albracht SP. An improved purification procedure for the soluble [NiFe]-hydrogenase of Ralstonia eutropha: new insights into its (in)stability and spectroscopic properties. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 11: 247-60. PMID 16418856 DOI: 10.1007/S00775-005-0075-4  0.402
2006 Albracht SP, Roseboom W, Hatchikian EC. The active site of the [FeFe]-hydrogenase from Desulfovibrio desulfuricans. I. Light sensitivity and magnetic hyperfine interactions as observed by electron paramagnetic resonance. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 11: 88-101. PMID 16323020 DOI: 10.1007/S00775-005-0039-8  0.428
2006 Roseboom W, De Lacey AL, Fernandez VM, Hatchikian EC, Albracht SP. The active site of the [FeFe]-hydrogenase from Desulfovibrio desulfuricans. II. Redox properties, light sensitivity and CO-ligand exchange as observed by infrared spectroscopy. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 11: 102-18. PMID 16323019 DOI: 10.1007/S00775-005-0040-2  0.408
2005 Volbeda A, Martin L, Cavazza C, Matho M, Faber BW, Roseboom W, Albracht SP, Garcin E, Rousset M, Fontecilla-Camps JC. Structural differences between the ready and unready oxidized states of [NiFe] hydrogenases. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 10: 591. PMID 27518782 DOI: 10.1007/S00775-005-0663-3  0.343
2005 Burgdorf T, Lenz O, Buhrke T, van der Linden E, Jones AK, Albracht SP, Friedrich B. [NiFe]-hydrogenases of Ralstonia eutropha H16: modular enzymes for oxygen-tolerant biological hydrogen oxidation. Journal of Molecular Microbiology and Biotechnology. 10: 181-96. PMID 16645314 DOI: 10.1159/000091564  0.334
2005 Burgdorf T, van der Linden E, Bernhard M, Yin QY, Back JW, Hartog AF, Muijsers AO, de Koster CG, Albracht SP, Friedrich B. The soluble NAD+-Reducing [NiFe]-hydrogenase from Ralstonia eutropha H16 consists of six subunits and can be specifically activated by NADPH. Journal of Bacteriology. 187: 3122-32. PMID 15838039 DOI: 10.1128/Jb.187.9.3122-3132.2005  0.366
2005 Burgdorf T, Löscher S, Liebisch P, Van der Linden E, Galander M, Lendzian F, Meyer-Klaucke W, Albracht SP, Friedrich B, Dau H, Haumann M. Structural and oxidation-state changes at its nonstandard Ni-Fe site during activation of the NAD-reducing hydrogenase from Ralstonia eutropha detected by X-ray absorption, EPR, and FTIR spectroscopy. Journal of the American Chemical Society. 127: 576-92. PMID 15643882 DOI: 10.1021/Ja0461926  0.364
2005 Roseboom W, Blokesch M, Böck A, Albracht SP. The biosynthetic routes for carbon monoxide and cyanide in the Ni-Fe active site of hydrogenases are different. Febs Letters. 579: 469-72. PMID 15642360 DOI: 10.1016/J.Febslet.2004.12.013  0.305
2004 Lyon EJ, Shima S, Boecher R, Thauer RK, Grevels FW, Bill E, Roseboom W, Albracht SP. Carbon monoxide as an intrinsic ligand to iron in the active site of the iron-sulfur-cluster-free hydrogenase H2-forming methylenetetrahydromethanopterin dehydrogenase as revealed by infrared spectroscopy. Journal of the American Chemical Society. 126: 14239-48. PMID 15506791 DOI: 10.1021/Ja046818S  0.38
2004 Blokesch M, Albracht SP, Matzanke BF, Drapal NM, Jacobi A, Böck A. The complex between hydrogenase-maturation proteins HypC and HypD is an intermediate in the supply of cyanide to the active site iron of [NiFe]-hydrogenases. Journal of Molecular Biology. 344: 155-67. PMID 15504408 DOI: 10.1016/J.Jmb.2004.09.040  0.381
2004 Bleijlevens B, Buhrke T, van der Linden E, Friedrich B, Albracht SP. The auxiliary protein HypX provides oxygen tolerance to the soluble [NiFe]-hydrogenase of ralstonia eutropha H16 by way of a cyanide ligand to nickel. The Journal of Biological Chemistry. 279: 46686-91. PMID 15342627 DOI: 10.1074/Jbc.M406942200  0.367
2004 Bleijlevens B, van Broekhuizen FA, De Lacey AL, Roseboom W, Fernandez VM, Albracht SP. The activation of the [NiFe]-hydrogenase from Allochromatium vinosum. An infrared spectro-electrochemical study. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 9: 743-52. PMID 15243788 DOI: 10.1007/S00775-004-0570-Z  0.384
2004 Van der Linden E, Burgdorf T, Bernhard M, Bleijlevens B, Friedrich B, Albracht SP. The soluble [NiFe]-hydrogenase from Ralstonia eutropha contains four cyanides in its active site, one of which is responsible for the insensitivity towards oxygen. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 9: 616-26. PMID 15164270 DOI: 10.1007/S00775-004-0555-Y  0.398
2004 van der Linden E, Faber BW, Bleijlevens B, Burgdorf T, Bernhard M, Friedrich B, Albracht SP. Selective release and function of one of the two FMN groups in the cytoplasmic NAD+-reducing [NiFe]-hydrogenase from Ralstonia eutropha. European Journal of Biochemistry / Febs. 271: 801-8. PMID 14764097 DOI: 10.1111/J.1432-1033.2004.03984.X  0.375
2003 Jones AK, Lamle SE, Pershad HR, Vincent KA, Albracht SP, Armstrong FA. Enzyme electrokinetics: electrochemical studies of the anaerobic interconversions between active and inactive states of Allochromatium vinosum [NiFe]-hydrogenase. Journal of the American Chemical Society. 125: 8505-14. PMID 12848556 DOI: 10.1021/Ja035296Y  0.38
2003 Chevallet M, Dupuis A, Issartel JP, Lunardi J, van Belzen R, Albracht SP. Two EPR-detectable [4Fe-4S] clusters, N2a and N2b, are bound to the NuoI (TYKY) subunit of NADH:ubiquinone oxidoreductase (Complex I) from Rhodobacter capsulatus. Biochimica Et Biophysica Acta. 1557: 51-66. PMID 12615348 DOI: 10.1016/S0005-2728(02)00398-5  0.414
2003 Albracht SP, van der Linden E, Faber BW. Quantitative amino acid analysis of bovine NADH:ubiquinone oxidoreductase (Complex I) and related enzymes. Consequences for the number of prosthetic groups. Biochimica Et Biophysica Acta. 1557: 41-9. PMID 12615347 DOI: 10.1016/S0005-2728(02)00393-6  0.392
2002 Léger C, Jones AK, Roseboom W, Albracht SP, Armstrong FA. Enzyme electrokinetics: hydrogen evolution and oxidation by Allochromatium vinosum [NiFe]-hydrogenase. Biochemistry. 41: 15736-46. PMID 12501202 DOI: 10.1021/Bi026586E  0.354
2002 Kurkin S, Meuer J, Koch J, Hedderich R, Albracht SP. The membrane-bound [NiFe]-hydrogenase (Ech) from Methanosarcina barkeri: unusual properties of the iron-sulphur clusters. European Journal of Biochemistry / Febs. 269: 6101-11. PMID 12473105 DOI: 10.1046/J.1432-1033.2002.03328.X  0.311
2002 Jones AK, Sillery E, Albracht SP, Armstrong FA. Direct comparison of the electrocatalytic oxidation of hydrogen by an enzyme and a platinum catalyst. Chemical Communications (Cambridge, England). 866-7. PMID 12123018 DOI: 10.1039/B201337A  0.331
2001 Buhrke T, Bleijlevens B, Albracht SP, Friedrich B. Involvement of hyp gene products in maturation of the H(2)-sensing [NiFe] hydrogenase of Ralstonia eutropha. Journal of Bacteriology. 183: 7087-93. PMID 11717266 DOI: 10.1128/Jb.183.24.7087-7093.2001  0.33
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  0.417
2001 Krieger CJ, Roseboom W, Albracht SP, Spormann AM. A stable organic free radical in anaerobic benzylsuccinate synthase of Azoarcus sp. strain T. The Journal of Biological Chemistry. 276: 12924-7. PMID 11278506 DOI: 10.1074/Jbc.M009453200  0.317
2000 Davidson G, Choudhury SB, Gu Z, Bose K, Roseboom W, Albracht SP, Maroney MJ. Structural examination of the nickel site in chromatium vinosum hydrogenase: redox state oscillations and structural changes accompanying reductive activation and CO binding. Biochemistry. 39: 7468-79. PMID 10858296 DOI: 10.1021/Bi000300T  0.34
2000 Happe RP, Roseboom W, Egert G, Friedrich CG, Massanz C, Friedrich B, Albracht SP. Unusual FTIR and EPR properties of the H2-activating site of the cytoplasmic NAD-reducing hydrogenase from Ralstonia eutropha. Febs Letters. 466: 259-63. PMID 10682839 DOI: 10.1016/S0014-5793(99)01799-8  0.326
1999 Gessner C, Stein M, Albracht SP, Lubitz W. Orientation-selected ENDOR of the active center in Chromatium vinosum [NiFe] hydrogenase in the oxidized "ready" state. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 4: 379-89. PMID 10555572 DOI: 10.1007/S007750050324  0.304
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  0.413
1999 Happe RP, Roseboom W, Albracht SP. Pre-steady-state kinetics of the reactions of [NiFe]-hydrogenase from Chromatium vinosum with H2 and CO. European Journal of Biochemistry / Febs. 259: 602-8. PMID 10092843 DOI: 10.1046/J.1432-1327.1999.00057.X  0.317
1999 Pierik AJ, Roseboom W, Happe RP, Bagley KA, Albracht SP. Carbon monoxide and cyanide as intrinsic ligands to iron in the active site of [NiFe]-hydrogenases. NiFe(CN)2CO, Biology's way to activate H2. The Journal of Biological Chemistry. 274: 3331-7. PMID 9920874 DOI: 10.1074/Jbc.274.6.3331  0.344
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  0.69
1998 Pierik AJ, Schmelz M, Lenz O, Friedrich B, Albracht SP. Characterization of the active site of a hydrogen sensor from Alcaligenes eutrophus. Febs Letters. 438: 231-5. PMID 9827551 DOI: 10.1016/S0014-5793(98)01306-4  0.362
1998 Kotlyar AB, Albracht SP, van Spanning RJ. Comparison of energization of complex I in membrane particles from Paracoccus denitrificans and bovine heart mitochondria. Biochimica Et Biophysica Acta. 1365: 53-9. PMID 9693721 DOI: 10.1016/S0005-2728(98)00042-5  0.414
1998 Bothe H, Darley DJ, Albracht SP, Gerfen GJ, Golding BT, Buckel W. Identification of the 4-glutamyl radical as an intermediate in the carbon skeleton rearrangement catalyzed by coenzyme B12-dependent glutamate mutase from Clostridium cochlearium. Biochemistry. 37: 4105-13. PMID 9521732 DOI: 10.1021/Bi971393Q  0.308
1997 van Belzen R, Kotlyar AB, Moon N, Dunham WR, Albracht SP. The iron-sulfur clusters 2 and ubisemiquinone radicals of NADH:ubiquinone oxidoreductase are involved in energy coupling in submitochondrial particles. Biochemistry. 36: 886-93. PMID 9020788 DOI: 10.1021/Bi9612982  0.38
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  0.365
1996 Müh U, Cinkaya I, Albracht SP, Buckel W. 4-Hydroxybutyryl-CoA dehydratase from Clostridium aminobutyricum: characterization of FAD and iron-sulfur clusters involved in an overall non-redox reaction. Biochemistry. 35: 11710-8. PMID 8794752 DOI: 10.1021/Bi9601363  0.438
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  0.698
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  0.34
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  0.404
1994 Bertram PA, Karrasch M, Schmitz RA, Böcher R, Albracht SP, Thauer RK. Formylmethanofuran dehydrogenases from methanogenic Archaea. Substrate specificity, EPR properties and reversible inactivation by cyanide of the molybdenum or tungsten iron-sulfur proteins. European Journal of Biochemistry / Febs. 220: 477-84. PMID 8125106 DOI: 10.1111/J.1432-1033.1994.Tb18646.X  0.366
1994 Lübben M, Arnaud S, Castresana J, Warne A, Albracht SP, Saraste M. A second terminal oxidase in Sulfolobus acidocaldarius. European Journal of Biochemistry / Febs. 224: 151-9. PMID 8076636 DOI: 10.1111/J.1432-1033.1994.Tb20006.X  0.343
1994 Bagley KA, Van Garderen CJ, Chen M, Duin EC, Albracht SP, Woodruff WH. Infrared studies on the interaction of carbon monoxide with divalent nickel in hydrogenase from Chromatium vinosum. Biochemistry. 33: 9229-36. PMID 8049224 DOI: 10.1021/Bi00197A026  0.309
1994 de Jong AM, Kotlyar AB, Albracht SP. Energy-induced structural changes in NADH:Q oxidoreductase of the mitochondrial respiratory chain. Biochimica Et Biophysica Acta. 1186: 163-71. PMID 8043590 DOI: 10.1016/0005-2728(94)90175-9  0.366
1993 Leguijt T, Engels PW, Crielaard W, Albracht SP, Hellingwerf KJ. Abundance, subunit composition, redox properties, and catalytic activity of the cytochrome bc1 complex from alkaliphilic and halophilic, photosynthetic members of the family Ectothiorhodospiraceae. Journal of Bacteriology. 175: 1629-36. PMID 8383662 DOI: 10.1128/Jb.175.6.1629-1636.1993  0.407
1992 Rospert S, Voges M, Berkessel A, Albracht SP, Thauer RK. Substrate-analogue-induced changes in the nickel-EPR spectrum of active methyl-coenzyme-M reductase from Methanobacterium thermoautotrophicum. European Journal of Biochemistry / Febs. 210: 101-7. PMID 1332856 DOI: 10.1111/J.1432-1033.1992.Tb17396.X  0.358
1992 van Belzen R, de Jong AM, Albracht SP. On the stoichiometry of the iron-sulphur clusters in mitochondrial NADH: ubiquinone oxidoreductase. European Journal of Biochemistry / Febs. 209: 1019-22. PMID 1330559 DOI: 10.1111/J.1432-1033.1992.Tb17377.X  0.385
1992 Schmitz RA, Albracht SP, Thauer RK. A molybdenum and a tungsten isoenzyme of formylmethanofuran dehydrogenase in the thermophilic archaeon Methanobacterium wolfei. European Journal of Biochemistry / Febs. 209: 1013-8. PMID 1330558 DOI: 10.1111/J.1432-1033.1992.Tb17376.X  0.377
1992 Schmitz RA, Albracht SP, Thauer RK. Properties of the tungsten-substituted molybdenum formylmethanofuran dehydrogenase from Methanobacterium wolfei. Febs Letters. 309: 78-81. PMID 1324851 DOI: 10.1016/0014-5793(92)80743-Z  0.344
1992 Michel C, Albracht SP, Buckel W. Adenosylcobalamin and cob(II)alamin as prosthetic groups of 2-methyleneglutarate mutase from Clostridium barkeri. European Journal of Biochemistry / Febs. 205: 767-73. PMID 1315277 DOI: 10.1111/J.1432-1033.1992.Tb16841.X  0.365
1992 Coremans JM, van Garderen CJ, Albracht SP. On the redox equilibrium between H2 and hydrogenase. Biochimica Et Biophysica Acta. 1119: 148-56. PMID 1311607 DOI: 10.1016/0167-4838(92)90385-Q  0.349
1988 Schulz H, Albracht SP, Coremans JM, Fuchs G. Purification and some properties of the corrinoid-containing membrane protein from Methanobacterium thermoautotrophicum. European Journal of Biochemistry / Febs. 171: 589-97. PMID 2831054 DOI: 10.1111/J.1432-1033.1988.Tb13829.X  0.304
1985 Schewe T, Albracht SP, Ludwig P, Rapoport SM. Two modes of irreversible inactivation of the mitochondrial electron-transfer system by tetradecanoic acid. Biochimica Et Biophysica Acta. 807: 210-5. PMID 2983761 DOI: 10.1016/0005-2728(85)90124-0  0.377
1985 van der Zwaan JW, Albracht SP, Fontijn RD, Slater EC. Monovalent nickel in hydrogenase from Chromatium vinosum. Light sensitivity and evidence for direct interaction with hydrogen. Febs Letters. 179: 271-7. PMID 2981705 DOI: 10.1016/0014-5793(85)80533-0  0.639
1985 Albracht S, Fontijn R, van der Zwaan J. Destruction and reconstitution of the activity of hydrogenase from Chromatium vinosum Biochimica Et Biophysica Acta (Bba) - Protein Structure and Molecular Enzymology. 832: 89-97. DOI: 10.1016/0167-4838(85)90177-3  0.428
1984 Albracht S, Van Der Zwaan J, Fontijn R. EPR Spectrum at 4, 9 and 35 GHz of hydrogenase from Chromatium vinosum. Direct evidence for spin-spin interaction between Ni(III) and the ironsulphur cluster Biochimica Et Biophysica Acta (Bba) - Bioenergetics. 766: 245-258. DOI: 10.1016/0005-2728(84)90238-X  0.4
1984 Unden G, Albracht S, Kröger A. Redox potentials and kinetic properties of fumarate reductase complex from Vibrio succinogenes Biochimica Et Biophysica Acta (Bba) - Bioenergetics. 767: 460-469. DOI: 10.1016/0005-2728(84)90044-6  0.425
1983 De Vries S, Albracht SP, Berden JA, Marres CA, Slater EC. The effect of pH, ubiquinone depletion and myxothiazol on the reduction kinetics of the prosthetic groups of ubiquinol:cytochrome c oxidoreductase. Biochimica Et Biophysica Acta. 723: 91-103. PMID 6299337 DOI: 10.1016/0005-2728(83)90013-0  0.724
1982 De Vries S, Albracht SP, Berden JA, Slater EC. The pathway of electrons through OH2:cytochrome c oxidoreductase studied by pre-steady -state kinetics. Biochimica Et Biophysica Acta. 681: 41-53. PMID 6288082 DOI: 10.1016/0005-2728(82)90276-6  0.73
1982 de Jong L, Albracht SP, Kemp A. Prolyl 4-hydroxylase activity in relation to the oxidation state of enzyme-bound iron. The role of ascorbate in peptidyl proline hydroxylation. Biochimica Et Biophysica Acta. 704: 326-32. PMID 6285984 DOI: 10.1016/0167-4838(82)90162-5  0.613
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  0.664
1981 de Vries S, Albracht SP, Berden JA, Slater EC. A new species of bound ubisemiquinone anion in QH2: cytochrome c oxidoreductase. The Journal of Biological Chemistry. 256: 11996-8. PMID 6271770  0.699
1981 van Heerikhuizen H, Albracht SP, Slater EC, van Rheenen PS. Purification and some properties of the soluble hydrogenase from Chromatium vinosum. Biochimica Et Biophysica Acta. 657: 26-39. PMID 6260199 DOI: 10.1016/0005-2744(81)90127-3  0.695
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  0.636
1979 de Vries S, Albracht SP. Intensity of highly anisotropic low-spin heme EPR signals. Biochimica Et Biophysica Acta. 546: 334-40. PMID 221015 DOI: 10.1016/0005-2728(79)90050-1  0.507
1979 de Vries S, Albracht SP, Leeuwerik FJ. The multiplicity and stoichiometry of the prosthetic groups in QH2: cytochrome c oxidoreductase as studied by EPR. Biochimica Et Biophysica Acta. 546: 316-33. PMID 221014 DOI: 10.1016/0005-2728(79)90049-5  0.596
1977 Albracht SP, Subramanian J. The number of Fe atoms in the iron-sulphur centers of the respiratory chain. Biochimica Et Biophysica Acta. 462: 36-48. PMID 199254 DOI: 10.1016/0005-2728(77)90187-6  0.4
1973 Dervartanian DV, Albracht SP, Berden JA, van Gelder BF, Slater EC. The EPR spectrum of isolated complex 3. Biochimica Et Biophysica Acta. 292: 496-501. PMID 4349922 DOI: 10.1016/0005-2728(73)90055-8  0.739
1972 Albracht SP, van Heerikhuizen H, Slater EC. Iron-sulphur proteins in the succinate oxidase system. Biochimica Et Biophysica Acta. 256: 1-13. PMID 4333297 DOI: 10.1016/0005-2728(72)90157-0  0.684
1972 Slater EC, Lee IY, van Gelder BF, Albracht SP, Berden JA. The effect of ATP on the EPR spectrum of phosphorylating sub-mitochondrial particles. Biochimica Et Biophysica Acta. 256: 14-23. PMID 4333296 DOI: 10.1016/0005-2728(72)90158-2  0.75
1971 Albracht SP, Van Heerikhuizen H, Slater EC. Succinate oxidase activity in the absence of ubiquinone. Febs Letters. 13: 265-266. PMID 11945682 DOI: 10.1016/0014-5793(71)80236-3  0.644
1971 Albracht SP, Slater EC. Effect of ATP on the EPR spectrum at 20 degrees K of phosphorylating sub-mitochondrial particles. Biochimica Et Biophysica Acta. 245: 508-11. PMID 4334352 DOI: 10.1016/0005-2728(71)90169-1  0.66
1971 Albracht SP, Slater EC. EPR studies at 20 degrees K on the mitochondrial respiratory chain. Biochimica Et Biophysica Acta. 245: 503-7. PMID 4334351 DOI: 10.1016/0005-2728(71)90168-X  0.663
1970 Albracht SP, Slater EC. Molybdenum associated with NADH dehydrogenase in complex I. Biochimica Et Biophysica Acta. 223: 457-9. PMID 5497668 DOI: 10.1016/0005-2728(70)90209-4  0.62
1969 Albracht SP, Slater EC. Reconstitutively active NADH dehydrogenase. Biochimica Et Biophysica Acta. 189: 308-10. PMID 4310792 DOI: 10.1016/0005-2728(69)90059-0  0.643
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