| Year |
Citation |
Score |
| 2011 |
Albracht SP, Meijer AJ, Rydström J. Mammalian NADH:ubiquinone oxidoreductase (Complex I) and nicotinamide nucleotide transhydrogenase (Nnt) together regulate the mitochondrial production of H₂O₂--implications for their role in disease, especially cancer. Journal of Bioenergetics and Biomembranes. 43: 541-64. PMID 21882037 DOI: 10.1007/S10863-011-9381-4 |
0.373 |
|
| 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 |
0.459 |
|
| 2010 |
Albracht SP. The reaction of NADPH with bovine mitochondrial NADH:ubiquinone oxidoreductase revisited: I. Proposed consequences for electron transfer in the enzyme. Journal of Bioenergetics and Biomembranes. 42: 261-78. PMID 20628895 DOI: 10.1007/S10863-010-9301-Z |
0.39 |
|
| 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 |
0.418 |
|
| 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 |
0.316 |
|
| 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 |
0.413 |
|
| 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 |
0.412 |
|
| 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 |
0.441 |
|
| 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 |
0.43 |
|
| 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 |
0.456 |
|
| 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 |
0.434 |
|
| 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 |
0.355 |
|
| 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 |
0.349 |
|
| 2005 |
Armstrong FA, Albracht SP. [NiFe]-hydrogenases: spectroscopic and electrochemical definition of reactions and intermediates. Philosophical Transactions. Series a, Mathematical, Physical, and Engineering Sciences. 363: 937-54; discussion 1. PMID 15991402 DOI: 10.1098/Rsta.2004.1528 |
0.387 |
|
| 2005 |
Lamle SE, Albracht SP, Armstrong FA. The mechanism of activation of a [NiFe]-hydrogenase by electrons, hydrogen, and carbon monoxide. Journal of the American Chemical Society. 127: 6595-604. PMID 15869280 DOI: 10.1021/Ja0424934 |
0.35 |
|
| 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 |
0.396 |
|
| 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 |
0.379 |
|
| 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 |
0.311 |
|
| 2004 |
Lamle SE, Albracht SP, Armstrong FA. Electrochemical potential-step investigations of the aerobic interconversions of [NiFe]-hydrogenase from Allochromatium vinosum: insights into the puzzling difference between unready and ready oxidized inactive states. Journal of the American Chemical Society. 126: 14899-909. PMID 15535717 DOI: 10.1021/Ja047939V |
0.334 |
|
| 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 |
0.401 |
|
| 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 |
0.408 |
|
| 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 |
0.392 |
|
| 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 |
0.408 |
|
| 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 |
0.421 |
|
| 2004 |
Kurkin S, George SJ, Thorneley RN, Albracht SP. Hydrogen-induced activation of the [NiFe]-hydrogenase from Allochromatium vinosum as studied by stopped-flow infrared spectroscopy. Biochemistry. 43: 6820-31. PMID 15157116 DOI: 10.1021/Bi049854C |
0.398 |
|
| 2004 |
George SJ, Kurkin S, Thorneley RN, Albracht SP. Reactions of H2, CO, and O2 with active [NiFe]-hydrogenase from Allochromatium vinosum. A stopped-flow infrared study. Biochemistry. 43: 6808-19. PMID 15157115 DOI: 10.1021/Bi049853K |
0.408 |
|
| 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 |
0.396 |
|
| 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 |
0.401 |
|
| 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 |
0.452 |
|
| 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 |
0.429 |
|
| 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 |
0.371 |
|
| 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 |
0.332 |
|
| 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 |
0.34 |
|
| 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 |
0.343 |
|
| 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 |
0.443 |
|
| 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 |
0.327 |
|
| 2000 |
Albracht SP, Hedderich R. Learning from hydrogenases: location of a proton pump and of a second FMN in bovine NADH--ubiquinone oxidoreductase (Complex I). Febs Letters. 485: 1-6. PMID 11086155 DOI: 10.1016/S0014-5793(00)02172-4 |
0.348 |
|
| 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 |
0.353 |
|
| 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 |
0.33 |
|
| 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 |
0.309 |
|
| 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 |
0.441 |
|
| 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 |
0.326 |
|
| 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 |
0.358 |
|
| 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 |
0.7 |
|
| 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 |
0.378 |
|
| 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 |
0.45 |
|
| 1998 |
Dupuis A, Darrouzet E, Duborjal H, Pierrard B, Chevallet M, van Belzen R, Albracht SP, Lunardi J. Distal genes of the nuo operon of Rhodobacter capsulatus equivalent to the mitochondrial ND subunits are all essential for the biogenesis of the respiratory NADH-ubiquinone oxidoreductase. Molecular Microbiology. 28: 531-41. PMID 9632256 DOI: 10.1046/J.1365-2958.1998.00814.X |
0.363 |
|
| 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 |
0.311 |
|
| 1997 |
Chevallet M, Dupuis A, Lunardi J, van Belzen R, Albracht SP, Issartel JP. The NuoI subunit of the Rhodobacter capsulatus respiratory Complex I (equivalent to the bovine TYKY subunit) is required for proper assembly of the membraneous and peripheral domains of the enzyme. European Journal of Biochemistry / Febs. 250: 451-8. PMID 9428698 DOI: 10.1111/J.1432-1033.1997.0451A.X |
0.321 |
|
| 1997 |
Speijer D, Breek CK, Muijsers AO, Hartog AF, Berden JA, Albracht SP, Samyn B, Van Beeumen J, Benne R. Characterization of the respiratory chain from cultured Crithidia fasciculata. Molecular and Biochemical Parasitology. 85: 171-86. PMID 9106191 DOI: 10.1016/S0166-6851(96)02823-X |
0.352 |
|
| 1997 |
Albracht SP, Mariette A, de Jong P. Bovine-heart NADH:ubiquinone oxidoreductase is a monomer with 8 Fe-S clusters and 2 FMN groups. Biochimica Et Biophysica Acta. 1318: 92-106. PMID 9030258 DOI: 10.1016/S0005-2728(96)00153-3 |
0.442 |
|
| 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 |
0.408 |
|
| 1996 |
Speijer D, Muijsers AO, Dekker H, de Haan A, Breek CK, Albracht SP, Benne R. Purification and characterization of cytochrome c oxidase from the insect trypanosomatid Crithidia fasciculata. Molecular and Biochemical Parasitology. 79: 47-59. PMID 8844671 DOI: 10.1016/0166-6851(96)02648-5 |
0.366 |
|
| 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 |
0.383 |
|
| 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 |
0.473 |
|
| 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 |
0.708 |
|
| 1996 |
Pfenninger-Li XD, Albracht SP, van Belzen R, Dimroth P. NADH:ubiquinone oxidoreductase of Vibrio alginolyticus: purification, properties, and reconstitution of the Na+ pump. Biochemistry. 35: 6233-42. PMID 8639563 DOI: 10.1021/Bi953032L |
0.412 |
|
| 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 |
0.35 |
|
| 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 |
0.434 |
|
| 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 |
0.39 |
|
| 1994 |
Hofmeister AE, Albracht SP, Buckel W. Iron-sulfur cluster-containing L-serine dehydratase from Peptostreptococcus asaccharolyticus: correlation of the cluster type with enzymatic activity. Febs Letters. 351: 416-8. PMID 8082806 DOI: 10.1016/0014-5793(94)00901-5 |
0.31 |
|
| 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 |
0.369 |
|
| 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 |
0.311 |
|
| 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 |
0.393 |
|
| 1994 |
De Jong AM, Albracht SP. Ubisemiquinones as obligatory intermediates in the electron transfer from NADH to ubiquinone. European Journal of Biochemistry / Febs. 222: 975-82. PMID 8026508 DOI: 10.1111/J.1432-1033.1994.Tb18948.X |
0.404 |
|
| 1994 |
Lübben M, Warne A, Albracht SP, Saraste M. The purified SoxABCD quinol oxidase complex of Sulfolobus acidocaldarius contains a novel haem. Molecular Microbiology. 13: 327-35. PMID 7984110 DOI: 10.1111/J.1365-2958.1994.Tb00426.X |
0.36 |
|
| 1994 |
Finel M, Majander AS, Tyynelä J, De Jong AM, Albracht SP, Wikström M. Isolation and characterisation of subcomplexes of the mitochondrial NADH:ubiquinone oxidoreductase (complex I). European Journal of Biochemistry / Febs. 226: 237-42. PMID 7957254 DOI: 10.1111/J.1432-1033.1994.0T237.X |
0.435 |
|
| 1993 |
Sorgenfrei O, Klein A, Albracht SP. Influence of illumination on the electronic interaction between 77Se and nickel in active F420-non-reducing hydrogenase from Methanococcus voltae. Febs Letters. 332: 291-7. PMID 8405473 DOI: 10.1016/0014-5793(93)80652-B |
0.374 |
|
| 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 |
0.438 |
|
| 1993 |
Albracht SP. Intimate relationships of the large and the small subunits of all nickel hydrogenases with two nuclear-encoded subunits of mitochondrial NADH: ubiquinone oxidoreductase. Biochimica Et Biophysica Acta. 1144: 221-4. PMID 8369340 DOI: 10.1016/0005-2728(93)90176-G |
0.333 |
|
| 1992 |
Coremans JM, van der Zwaan JW, Albracht SP. Distinct redox behaviour of prosthetic groups in ready and unready hydrogenase from Chromatium vinosum. Biochimica Et Biophysica Acta. 1119: 157-68. PMID 1540647 DOI: 10.1016/0167-4838(92)90386-R |
0.388 |
|
| 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 |
0.38 |
|
| 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 |
0.415 |
|
| 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 |
0.405 |
|
| 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 |
0.363 |
|
| 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 |
0.388 |
|
| 1992 |
Hedderich R, Albracht SP, Linder D, Koch J, Thauer RK. Isolation and characterization of polyferredoxin from Methanobacterium thermoautotrophicum. The mvhB gene product of the methylviologen-reducing hydrogenase operon. Febs Letters. 298: 65-8. PMID 1312016 DOI: 10.1016/0014-5793(92)80023-A |
0.357 |
|
| 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 |
0.363 |
|
| 1991 |
Rospert S, Böcher R, Albracht SP, Thauer RK. Methyl-coenzyme M reductase preparations with high specific activity from H2-preincubated cells of Methanobacterium thermoautotrophicum. Febs Letters. 291: 371-5. PMID 1657649 DOI: 10.1016/0014-5793(91)81323-Z |
0.355 |
|
| 1990 |
Lauterbach F, Körtner C, Albracht SP, Unden G, Kröger A. The fumarate reductase operon of Wolinella succinogenes. Sequence and expression of the frdA and frdB genes. Archives of Microbiology. 154: 386-93. PMID 2244791 DOI: 10.1007/Bf00276536 |
0.33 |
|
| 1990 |
van der Zwaan JW, Coremans JM, Bouwens EC, Albracht SP. Effect of 17O2 and 13CO on EPR spectra of nickel in hydrogenase from Chromatium vinosum. Biochimica Et Biophysica Acta. 1041: 101-10. PMID 2176104 DOI: 10.1016/0167-4838(90)90051-G |
0.373 |
|
| 1990 |
Stupperich E, Eisinger HJ, Albracht SP. Evidence for a super-reduced cobamide as the major corrinoid fraction in vivo and a histidine residue as a cobalt ligand of the p-cresolyl cobamide in the acetogenic bacterium Sporomusa ovata. European Journal of Biochemistry / Febs. 193: 105-9. PMID 2171927 DOI: 10.1111/J.1432-1033.1990.Tb19310.X |
0.325 |
|
| 1990 |
van Belzen R, van Gaalen MC, Cuypers PA, Albracht SP. New evidence for the dimeric nature of NADH:Q oxidoreductase in bovine-heart submitochondrial particles. Biochimica Et Biophysica Acta. 1017: 152-9. PMID 2112409 DOI: 10.1016/0005-2728(90)90146-U |
0.36 |
|
| 1989 |
van Belzen R, Albracht SP. The pathway of electron transfer in NADH:Q oxidoreductase. Biochimica Et Biophysica Acta. 974: 311-20. PMID 2499359 DOI: 10.1016/S0005-2728(89)80249-X |
0.423 |
|
| 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 |
0.317 |
|
| 1987 |
Van der Zwaan JW, Albracht SP, Fontijn RD, Mul P. On the anomalous temperature behaviour of the EPR signal of monovalent nickel in hydrogenase. European Journal of Biochemistry / Febs. 169: 377-84. PMID 2826142 DOI: 10.1111/J.1432-1033.1987.Tb13623.X |
0.361 |
|
| 1986 |
Albracht SP, Bakker PT. Evidence for two independent pathways of electron transfer in mitochondrial NADH:Q oxidoreductase. II. Kinetics of reoxidation of the reduced enzyme. Biochimica Et Biophysica Acta. 850: 423-8. PMID 3015207 DOI: 10.1016/0005-2728(86)90110-6 |
0.387 |
|
| 1986 |
Bakker PT, Albracht SP. Evidence for two independent pathways of electron transfer in mitochondrial NADH:Q oxidoreductase. I. Pre-steady-state kinetics with NADPH. Biochimica Et Biophysica Acta. 850: 413-22. PMID 3015206 DOI: 10.1016/0005-2728(86)90109-X |
0.401 |
|
| 1986 |
van der Zwaan J, Albracht S, Fontijn R, Roelofs Y. EPR evidence for direct interaction of carbon monoxide with nickel in hydrogenase from Chromatium vinosum Biochimica Et Biophysica Acta (Bba) - Protein Structure and Molecular Enzymology. 872: 208-215. DOI: 10.1016/0167-4838(86)90273-6 |
0.364 |
|
| 1986 |
Albracht S, Kröger A, van der Zwaan J, Unden G, Böcher R, Mell H, Fontijn R. Direct evidence for sulphur as a ligand to nickel in hydrogenase: an EPR study of the enzyme from Wolinella succinogenes enriched in 33S Biochimica Et Biophysica Acta (Bba) - Protein Structure and Molecular Enzymology. 874: 116-127. DOI: 10.1016/0167-4838(86)90108-1 |
0.395 |
|
| 1986 |
Albracht S, Ankel-Fuchs D, Van der Zwaan J, Fontijn R, Thauer R. A new EPR signal of nickel in Methanobacterium thermoautotrophicum Biochimica Et Biophysica Acta (Bba) - Protein Structure and Molecular Enzymology. 870: 50-57. DOI: 10.1016/0167-4838(86)90007-5 |
0.355 |
|
| 1985 |
Albracht SP. The use of electron-paramagnetic-resonance spectroscopy to establish the properties of nickel and the iron-sulphur cluster in hydrogenase from Chromatium vinosum. Biochemical Society Transactions. 13: 582-5. PMID 2993066 DOI: 10.1042/Bst0130582 |
0.346 |
|
| 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 |
0.403 |
|
| 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 |
0.643 |
|
| 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 |
0.461 |
|
| 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 |
0.426 |
|
| 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 |
0.459 |
|
| 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 |
0.734 |
|
| 1982 |
Beinert H, Albracht SP. New insights, ideas and unanswered questions concerning iron-sulfur clusters in mitochondria. Biochimica Et Biophysica Acta. 683: 245-77. PMID 6297553 DOI: 10.1016/0304-4173(82)90003-9 |
0.344 |
|
| 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 |
0.74 |
|
| 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 |
0.631 |
|
| 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 |
0.67 |
|
| 1982 |
Albracht SP, Unden G, Kröger A. Iron-sulphur clusters in fumarate reductase from Vibrio succinogenes. Biochimica Et Biophysica Acta. 661: 295-302. PMID 6271222 DOI: 10.1016/0005-2744(81)90018-8 |
0.414 |
|
| 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 |
0.704 |
|
| 1981 |
Schewe T, Albracht SP, Ludwig P. On the site of action of the inhibition of the mitochondrial respiratory chain by lipoxygenase. Biochimica Et Biophysica Acta. 636: 210-7. PMID 6269601 DOI: 10.1016/0005-2728(81)90095-5 |
0.428 |
|
| 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 |
0.712 |
|
| 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 |
0.639 |
|
| 1980 |
Albracht SP. The prosthetic groups in succinate dehydrogenase. Number and stoichiometry. Biochimica Et Biophysica Acta. 612: 11-28. PMID 6244847 DOI: 10.1016/0005-2744(80)90274-0 |
0.409 |
|
| 1979 |
Albracht SP, Leeuwerik FJ, van Swol B. The stoichiometry of the iron-sulphur clusters 1a, 1b and 2 of NADH:Q oxidoreductase as present in beef-heart submitochondrial particles. Febs Letters. 104: 197-200. PMID 225201 DOI: 10.1016/0014-5793(79)81114-X |
0.335 |
|
| 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 |
0.503 |
|
| 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 |
0.609 |
|
| 1979 |
Heidrich HG, Albracht SP, Bäckstrom D. Two iron-sulfur centers in mitochondrial outer membranes from beef heart as prepared by free-flow electrophoresis. Febs Letters. 95: 314-8. PMID 214348 DOI: 10.1016/0014-5793(78)81019-9 |
0.313 |
|
| 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 |
0.423 |
|
| 1977 |
Albracht SP, Dooijewaard G, Leeuwerik FJ, Swol BV. EPR signals of NADH: Q oxidoreductase. Shape and intensity. Biochimica Et Biophysica Acta. 459: 300-17. PMID 189811 DOI: 10.1016/0005-2728(77)90030-5 |
0.376 |
|
| 1975 |
Albracht SP, Heidrich HG. Beef-heart submitochondrial particles: a mixture of mitochondrial inner and outer membranes. Biochimica Et Biophysica Acta. 376: 231-6. PMID 163647 DOI: 10.1016/0005-2728(75)90014-6 |
0.317 |
|
| 1974 |
Albracht SP. Some new paramagnetic centers in submitochondrial particles detectable by EPR spectroscopy. Biochimica Et Biophysica Acta. 347: 183-92. PMID 4152157 DOI: 10.1016/0005-2728(74)90043-7 |
0.381 |
|
| 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 |
0.743 |
|
| 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 |
0.693 |
|
| 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 |
0.757 |
|
| 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 |
0.647 |
|
| 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 |
0.668 |
|
| 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 |
0.67 |
|
| 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 |
0.626 |
|
| 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 |
0.647 |
|
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