Search Results - "Albracht, S P"

Abundance, subunit composition, redox properties, and catalytic activity of the cytochrome bc1 complex from alkaliphilic and halophilic, photosynthetic members of the family Ectothiorhodospiraceae by LEGUIJT, T, ENGELS, P. W, CRIELAARD, W, ALBRACHT, S. P. J, HELLINGWERF, K. J

“…Article Usage Stats Services JB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley…”
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Orientation-selected ENDOR of the active center in Chromatium vinosum [NiFe] hydrogenase in the oxidized "ready" state by Gessner, C, Stein, M, Albracht, S P, Lubitz, W

“…Electron nuclear double resonance (ENDOR) was applied to study the active site of the oxidized "ready" state, Ni(r), in the [NiFe] hydrogenase of Chromatium…”
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A new species of bound ubisemiquinone anion in QH2: cytochrome c oxidoreductase by de Vries, S, Albracht, S P, Berden, J A, Slater, E C

“…Using a combination of EPR and low temperature diffuse reflectance spectroscopy, a new species of semiquinone anion has been detected in QH2:cytochrome c…”
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Resolution of NADH:ubiquinone oxidoreductase from bovine heart mitochondria into two subcomplexes, one of which contains the redox centers of the enzyme by Finel, Moshe, Skehel, J. Mark, Albracht, Simon P. J, Fearnley, Ian M, Walker, John E

“…NADH:ubiquinone oxidoreductase (complex I) was purified from bovine heart mitochondria by solubilization with n-dodecyl beta-D-maltoside (lauryl maltoside),…”
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Further characterization of the spin coupling observed in oxidized hydrogenase from Chromatium vinosum. A Mössbauer and multifrequency EPR study by SURERUS, K. K, MIN CHEN, VAN DER ZWAAN, J. W, RUSNAK, F. M, KOLK, M, DUIN, E. C, ALBRACHT, S. P. J, MÜNCK, E

“…Hydrogenase from Chromatium vinosum contains 1 Ni, 11-12 Fe, and ca. 9 sulfides. EPR and Mössbauer studies of the enzyme prepared in four different oxidation…”
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Methyl‐coenzyme M reductase preparations with high specific activity from H2‐preincubated cells of Methanobacterium thermoautotrophicum by Rospert, S., Böcher, R., Albracht, S.P.J., Thauer, R.K.

“…The study of the nickel enzyme methyl‐coenzyme M reductase from methanogenic bacteria has been hampered until now by the fact that upon cell rupture the…”
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Identification of a paramagnetic species as an early intermediate in the coenzyme B12‐dependent glutamate mutase reaction A cob(II)amide? by Leutbecher, U., Albracht, S.P.J., Buckel, W.

“…Highly active and cobamide‐free glutamate mutase was obtained from Clostridium cochlearium by a modification of the original purification procedure. After…”
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Nickel hydrogenases: in search of the active site by Albracht, S P

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Properties of the tungsten-substituted molybdenum formylmethanofuran dehydrogenase from Methanobacterium wolfei by Schmitz, R.A., Albracht, S.P.J., Thauer, R.K.

“…In Methanobacterium wolfei two formylmethanofuran dehydrogenases are present, one of which is a molybdenum- and the other a tungsten enzyme. We report here…”
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Monovalent nickel in hydrogenase from Chromatium vinosum: Light sensitivity and evidence for direct interaction with hydrogen by van der Zwaan, J.W., Albracht, S.P.J., Fontijn, R.D., Slater, E.C.

“…Redox titrations with hydrogenase from Chromatium vinosum show that its nickel ion can exist in 3, possibly 4, different redox states: the 3 +, 2 +, 1 + and…”
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The fumarate reductase operon of Wolinella succinogenes. Sequence and expression of the frdA and frdB genes by Lauterbach, F, Körtner, C, Albracht, S P, Unden, G, Kröger, A

“…The genes of the fumarate reductase of Wolinella succinogenes are organized in an operon. The three structural genes in the order frdC, frdA, frdB, are…”
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Energy-induced structural changes in NADH:Q oxidoreductase of the mitochondrial respiratory chain by de Jong, A M, Kotlyar, A B, Albracht, S P

“…The reaction of coupled submitochondrial particles (SMP) with NADH was studied in the absence and presence of the uncoupler gramicidin, both in…”
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Influence of illumination on the electronic interaction between 77Se and nickel in active F420‐non‐reducing hydrogenase from Methanococcus voltae by Sorgenfrei, Oliver, Klein, Albrecht, Albracht, Simon P.J.

“…The selenium‐containing F420‐non‐reducing hydrogenase from Methanococcus voltae was anaerobically purified. The enzyme as isolated showed an EPR spectrum with…”
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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 by Pierik, A J, Roseboom, W, Happe, R P, Bagley, K A, Albracht, S P

“…Infrared-spectroscopic studies on the [NiFe]-hydrogenase of Chromatium vinosum-enriched in 15N or 13C, as well as chemical analyses, show that this enzyme…”
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Biological activation of hydrogen by Happe, R P, Roseboom, W, Pierik, A J, Albracht, S P, Bagley, K A

“…Hydrogenases are enzymes that can reversibly split molecular hydrogen. In Ni/Fe hydrogenases, the nickel atom and a nearby iron atom form the site of hydrogen…”
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Distinct redox behaviour of prosthetic groups in ready and unready hydrogenase from Chromatium vinosum by Coremans, J M, van der Zwaan, J W, Albracht, S P

“…The redox behaviour of the Ni(III)/Ni(II) transition in hydrogenase from Chromatium vinosum is described and compared with the redox behaviour of the nickel…”
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A molybdenum and a tungsten isoenzyme of formylmethanofuran dehydrogenase in the thermophilic archaeon Methanobacterium wolfei by SCHMITZ, Ruth A., ALBRACHT, Simon P. J., THAUER, Rudolf K.

“…We have recently reported that the thermophilic archaeon Methanobacterium wolfei contains two formylmethanofuran dehydrogenases, I and II. Formylmethanofuran…”
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New evidence for the dimeric nature of NADH:Q oxidoreductase in bovine-heart submitochondrial particles by van Belzen, R, van Gaalen, M C, Cuypers, P A, Albracht, S P

“…The initial velocity of NADH oxidation by bovine-heart submitochondrial particles was measured at pH 8.0 after pretreatment of these particles with different…”
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Learning from hydrogenases: location of a proton pump and of a second FMN in bovine NADH–ubiquinone oxidoreductase (Complex I) by Albracht, Simon P.J., Hedderich, Reiner

“…Hydrogenases have clear evolutionary links to the much more complex NADH–ubiquinone oxidoreductases (Complex I). Certain membrane-bound [NiFe]-hydrogenases…”
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Adenosylcobalamin and cob(II)alamin as prosthetic groups of 2‐methyleneglutarate mutase from Clostridium barkeri by MICHEL, Christoph, ALBRACHT, Simon P. J., BUCKEL, Wolfgang

“…The ultraviolet/visible spectrum of the pure pink‐orange 2‐methyleneglutarate mutase from Clostridium barkeri between 300–600 nm showed the presence of…”
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