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Results: 1-16 |
Results: 16
Plant adenosine 5 '-phospho sulfate reductase is a novel iron-sulfur protein
Authors: Kopriva, S Buchert, T Fritz, G Suter, M Weber, M Benda, R Schaller, J Feller, U Schurmann, P Schunemann, V Trautwein, AX Kroneck, PMH Brunold, C
Citation: S. Kopriva et al., Plant adenosine 5 '-phospho sulfate reductase is a novel iron-sulfur protein, J BIOL CHEM, 276(46), 2001, pp. 42881-42886
Spectroscopic investigation and determination of reactivity and structure of the tetraheme cytochrome c(3) from Desulfovibrio desulfuricans Essex 6
Authors: Einsle, O Foerster, S Mann, K Fritz, G Messerschmidt, A Kroneck, PMH
Citation: O. Einsle et al., Spectroscopic investigation and determination of reactivity and structure of the tetraheme cytochrome c(3) from Desulfovibrio desulfuricans Essex 6, EUR J BIOCH, 268(10), 2001, pp. 3028-3035
Three-dimensional structure of the nonaheme cytochrome c from Desulfovibrio desulfuricans Essex in the Fe(III) state at 1.89 angstrom resolution
Authors: Umhau, S Fritz, G Diederichs, K Breed, J Welte, W Kroneck, PMH
Citation: S. Umhau et al., Three-dimensional structure of the nonaheme cytochrome c from Desulfovibrio desulfuricans Essex in the Fe(III) state at 1.89 angstrom resolution, BIOCHEM, 40(5), 2001, pp. 1308-1316
Nonaheme cytochrome c, a new physiological electron acceptor for [Ni,Fe] hydrogenase in the sulfate-reducing bacterium Desulfovibrio desulfuricans Essex: Primary sequence, molecular parameters, and redox properties
Authors: Fritz, G Griesshaber, D Seth, O Kroneck, PMH
Citation: G. Fritz et al., Nonaheme cytochrome c, a new physiological electron acceptor for [Ni,Fe] hydrogenase in the sulfate-reducing bacterium Desulfovibrio desulfuricans Essex: Primary sequence, molecular parameters, and redox properties, BIOCHEM, 40(5), 2001, pp. 1317-1324
A NapC/NirT-type cytochrome c (NrfH) is the mediator between the quinone pool and the cytochrome c nitrite reductase of Wolinella succinogenes
Authors: Simon, J Gross, R Einsle, O Kroneck, PMH Kroger, A Klimmek, O
Citation: J. Simon et al., A NapC/NirT-type cytochrome c (NrfH) is the mediator between the quinone pool and the cytochrome c nitrite reductase of Wolinella succinogenes, MOL MICROB, 35(3), 2000, pp. 686-696
Crystallization and preliminary X-ray analysis of adenylylsulfate reductase from Archaeoglobus fulgidus
Authors: Roth, A Fritz, G Buchert, T Huber, H Stetter, KO Ermler, U Kroneck, PMH
Citation: A. Roth et al., Crystallization and preliminary X-ray analysis of adenylylsulfate reductase from Archaeoglobus fulgidus, ACT CRYST D, 56, 2000, pp. 1673-1675
Bacterial cytochrome c nitrite reductase: new structural and functional aspects
Authors: Stach, P Einsle, O Schumacher, W Kurun, E Kroneck, PMH
Citation: P. Stach et al., Bacterial cytochrome c nitrite reductase: new structural and functional aspects, J INORG BIO, 79(1-4), 2000, pp. 381-385
Cytochrome c nitrite reductase from Wolinella succinogenes - Structure at 1.6 angstrom resolution, inhibitor binding, and heme-packing motifs
Authors: Einsle, O Stach, P Messerschmidt, A Simon, J Kroger, A Huber, R Kroneck, PMH
Citation: O. Einsle et al., Cytochrome c nitrite reductase from Wolinella succinogenes - Structure at 1.6 angstrom resolution, inhibitor binding, and heme-packing motifs, J BIOL CHEM, 275(50), 2000, pp. 39608-39616
Adenylylsulfate reductases from archaea and bacteria are 1 : 1 alpha beta-heterodimeric iron-sulfur flavoenzymes - high similarity of molecular properties emphasizes their central role in sulfur metabolism
Authors: Fritz, G Buchert, T Huber, H Stetter, KO Kroneck, PMH
Citation: G. Fritz et al., Adenylylsulfate reductases from archaea and bacteria are 1 : 1 alpha beta-heterodimeric iron-sulfur flavoenzymes - high similarity of molecular properties emphasizes their central role in sulfur metabolism, FEBS LETTER, 473(1), 2000, pp. 63-66
Structural investigations of the Cu-A centre of nitrous oxide reductase from Pseudomonas stutzeri by site-directed mutagenesis and X-ray absorption spectroscopy
Authors: Charnock, JM Dreusch, A Korner, H Neese, F Nelson, J Kannt, A Michel, H Garner, CD Kroneck, PMH Zumft, WG
Citation: Jm. Charnock et al., Structural investigations of the Cu-A centre of nitrous oxide reductase from Pseudomonas stutzeri by site-directed mutagenesis and X-ray absorption spectroscopy, EUR J BIOCH, 267(5), 2000, pp. 1368-1381
Structural investigations of the Cu-A center of nitrous oxide reductase from Pseudomonas stutzeri by site-directed mutagenesis and X-ray absorption spectroscopy (vol 267, pg 1368, 2000)
Authors: Charnock, JM Dreusch, A Korner, H Neese, F Nelson, J Kannt, A Michel, H Garner, CD Kroneck, PMH Zumft, WG
Citation: Jm. Charnock et al., Structural investigations of the Cu-A center of nitrous oxide reductase from Pseudomonas stutzeri by site-directed mutagenesis and X-ray absorption spectroscopy (vol 267, pg 1368, 2000), EUR J BIOCH, 267(21), 2000, pp. 6509-6509
Structure of cytochrome c nitrite reductase
Authors: Einsle, O Messerschmidt, A Stach, P Bourenkov, GP Bartunik, HD Huber, R Kroneck, PMH
Citation: O. Einsle et al., Structure of cytochrome c nitrite reductase, NATURE, 400(6743), 1999, pp. 476-480
Acetylene hydratase of Pelobacter acetylenicus - Molecular and spectroscopic properties of the tungsten iron-sulfur enzyme
Authors: Meckenstock, RU Krieger, R Ensign, S Kroneck, PMH Schink, B
Citation: Ru. Meckenstock et al., Acetylene hydratase of Pelobacter acetylenicus - Molecular and spectroscopic properties of the tungsten iron-sulfur enzyme, EUR J BIOCH, 264(1), 1999, pp. 176-182
A structural comparison of molybdenum cofactor-containing enzymes
Authors: Kisker, C Schindelin, H Baas, D Retey, J Meckenstock, RU Kroneck, PMH
Citation: C. Kisker et al., A structural comparison of molybdenum cofactor-containing enzymes, FEMS MIC R, 22(5), 1998, pp. 503-521
Probing the structure of the human Ca2+- and Zn2+-binding protein S100A3: spectroscopic investigations of its transition metal ion complexes, and three-dimensional structural model
Authors: Fritz, G Heizmann, CW Kroneck, PMH
Citation: G. Fritz et al., Probing the structure of the human Ca2+- and Zn2+-binding protein S100A3: spectroscopic investigations of its transition metal ion complexes, and three-dimensional structural model, BBA-MOL CEL, 1448(2), 1998, pp. 264-276
Electron paramagnetic resonance power studies on the mixed-valence electron transfer centre of nitrous oxide reductase: presence of a modified Cu-A site in the enzyme from Pseudomonas stutzeri
Authors: Antholine, WE Kroneck, PMH Zumft, WG
Citation: We. Antholine et al., Electron paramagnetic resonance power studies on the mixed-valence electron transfer centre of nitrous oxide reductase: presence of a modified Cu-A site in the enzyme from Pseudomonas stutzeri, MOLEC PHYS, 95(6), 1998, pp. 1247-1253
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