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Université de Neuchâtel

Role of Histidine-86 in the Catalytic Mechanism of Ferredoxin: Thioredoxin Reductase

Walters, Elizabeth M. ; Garcia-Serres, Ricardo ; Naik, Sunil G. ; Bourquin, Florence ; Glauser, Dominique A. ; Schürmann, Peter ; Huynh, Boi Hanh ; Johnson, Michael K.

In: Biochemistry, 2009, vol. 48, no. 5, p. 1016-1024

Ferredoxin:thioredoxin reductase catalyzes the reduction of thioredoxins in plant chloroplasts using the [Fe2S2] ferredoxin as a one-electron donor and as such plays a central role in light regulation of oxygenic photosynthesis. The active-site comprises a [Fe4S4] cluster next to a redox-active disulfide that is cleaved in sequential one-electron steps...

Université de Neuchâtel

The Function and Properties of the Iron−Sulfur Center in Spinach Ferredoxin:Thioredoxin Reductase: A New Biological Role for Iron−Sulfur Clusters

Staples, Christopher R. ; Ameyibor, Emmanuel ; Fu, Weiguang ; Gardet-Salvi, Laura ; Stritt-Etter, Anne-Lise ; Schürmann, Peter ; Knaff, David B. ; Johnson, Michael K.

In: Biochemistry, 1991, vol. 35, no. 35, p. 11425–11434

Thioredoxin reduction in chloroplasts is catalyzed by a unique class of disulfide reductases which use a [2Fe-2S]2+/+ ferredoxin as the electron donor and contain an Fe-S cluster as the sole prosthetic group in addition to the active-site disulfide. The nature, properties, and function of the Fe-S cluster in spinach ferredoxin:thioredoxin reductase (FTR) have been investigated by the...

Université de Neuchâtel

Role of the [Fe4S4] Cluster in Mediating Disulfide Reduction in Spinach Ferredoxin:Thioredoxin Reductase

Staples, Christopher R. ; Gaymard, Eric ; Stritt-Etter, Anne-Lise ; Telser, Joshua ; Hoffman, Brian M. ; Schürmann, Peter ; Knaff, David B. ; Johnson, Michael K.

In: Biochemistry, 1998, vol. 37, no. 13, p. 4612–4620

Thioredoxin reduction in plant chloroplasts is catalyzed by a unique class of disulfide reductases which use a one-electron donor, [Fe2S2]2+,+ ferredoxin, and has an active site involving a disulfide in close proximity to a [Fe4S4]2+ cluster. In this study, spinach ferredoxin:thioredoxin reductase (FTR) reduced with stoichiometric...

Université de Neuchâtel

Spectroscopic Characterization of Site-Specific [Fe4S4] Cluster Chemistry in Ferredoxin:Thioredoxin Reductase: Implications for the Catalytic Mechanism

Walters, Elizabeth M. ; Garcia-Serres, Ricardo ; Jameson, Guy N. L. ; Glauser, Dominique A. ; Bourquin, Florence ; Manieri, Wanda ; Schürmann, Peter ; Johnson, Michael K. ; Huynh, Boi Hanh

In: Journal of the American Chemical Society (JACS), 2005, vol. 127, no. 26, p. 9612–9624

Light regulation of enzyme activities in oxygenic photosynthesis is mediated by ferredoxin:thioredoxin reductase (FTR), a novel class of disulfide reductase with an active site comprising a [Fe4S4]2+ cluster and an adjacent disulfide, that catalyzes reduction of the thioredoxin disulfide in two sequential one-electron steps using a...

Université de Neuchâtel

Spectroscopic Evidence for Site Specific Chemistry at a Unique Iron Site of the [4Fe−4S] Cluster in Ferredoxin:Thioredoxin Reductase

Jameson, Guy N. L. ; Walters, Elizabeth M. ; Manieri, Wanda ; Schürmann, Peter ; Johnson, Michael K. ; Hanh Huynh, Boi

In: Journal of the American Chemical Society (JACS), 2003, vol. 125, no. 5, p. 1146–1147

Ferredoxin:thioredoxin reductase (FTR) catalyzes the reduction of the disulfide in thioredoxin in two one-electron steps using an active site comprising a [4Fe−4S] in close proximity to a redox active disulfide. Mössbauer spectroscopy has been used to investigate the ligation and electronic properties of the [4Fe−4S] cluster in as-prepared FTR which has the active-site disulfide intact and...

Université de Neuchâtel

Characterization of Tic110, a Channel-forming Protein at the Inner Envelope Membrane of Chloroplasts, Unveils a Response to Ca2+ and a Stromal Regulatory Disulfide Bridge

Balsera, Mónica ; Goetze, Tom A. ; Kovács-Bogdán, Erika ; Schürmann, Peter ; Wagner, Richard ; Buchanan, Bob B. ; Soll, Jürgen ; Bölter, Bettina

In: Journal of Biological Chemistry, 2009, vol. 284, no. 5, p. 2603-2616

Tic110 has been proposed to be a channel-forming protein at the inner envelope of chloroplasts whose function is essential for the import of proteins synthesized in the cytosol. Sequence features and topology determination experiments presently summarized suggest that Tic110 consists of six transmembrane helices. Its topology has been mapped by limited proteolysis experiments in combination with...

Université de Neuchâtel

Structural snapshots along the reaction pathway of ferredoxin–thioredoxin reductase

Dai, Shaodong ; Glauser, Dominique A. ; Bourquin, Florence ; Manieri, Wanda ; Schürmann, Peter ; Eklund, Hans

In: Nature, 2007, vol. 448, p. 92-96

Oxygen-evolving photosynthetic organisms regulate carbon metabolism through a light-dependent redox signalling pathway1. Electrons are shuttled from photosystem I by means of ferredoxin (Fdx) to ferredoxin–thioredoxin reductase (FTR), which catalyses the two-electron-reduction of chloroplast thioredoxins (Trxs). These modify target enzyme activities by reduction, regulating carbon flow2. FTR is...

Université de Neuchâtel

Inhibition of Escherichia coli porphobilinogen synthase using analogs of postulated intermediates

Jarret, Caroline ; Stauffer, Frédéric ; Henz, Matthias E ; Marty, Maurus ; Lüönd, Rainer M ; Bobálová, Janette ; Schürmann, Peter ; Neier, Reinhard

In: Chemistry & Biology, 2000, vol. 7, no. 3, p. 185-196

Background: Porphobilinogen synthase is the second enzyme involved in the biosynthesis of natural tetrapyrrolic compounds, and condenses two molecules of 5-aminolevulinic acid (ALA) through a nonsymmetrical pathway to form porphobilinogen. Each substrate is recognized individually at two different active site positions to be regioselectively introduced into the product. According to...

Université de Neuchâtel

Characterization of Ferredoxin:Thioredoxin Reductase Modified by Site-directed Mutagenesis

Glauser, Dominique A. ; Bourquin, Florence ; Manieri, Wanda ; Schürmann, Peter

In: The Journal of Biological Chemistry, 2004, vol. 277, no. 24, p. 16662-16669

Ferredoxin:thioredoxin reductase (FTR) is a key regulatory enzyme of oxygenic photosynthetic cells involved in the reductive regulation of important target enzymes. It catalyzes the two-electron reduction of the disulfide of thioredoxins with electrons from ferredoxin involving a 4Fe-4S cluster and an adjacent active-site disulfide. We replaced Cys-57, Cys-87, and His-86 in the active site of...

Université de Neuchâtel

Adenosine 5'-Phosphosulfate Sulfotransferase and Adenosine 5'-Phosphosulfate Reductase Are Identical Enzymes

Suter, Marianne ; von Ballmoos, Peter ; Kopriva, Stanislav ; Op den Camp, Roel ; Schaller, Johann ; Kuhlemeier, Cris ; Schürmann, Peter ; Brunold, Christian

In: The Journal of Biological Chemistry, 2000, vol. 275, no. 2, p. 930-936

Adenosine 5'-phosphosulfate (APS) sulfotransferase and APS reductase have been described as key enzymes of assimilatory sulfate reduction of plants catalyzing the reduction of APS to bound and free sulfite, respectively. APS sulfotransferase was purified to homogeneity from Lemna minor and compared with APS reductase previously obtained by functional complementation of a mutant strain of...