Affiner les résultats

Type de document

Collection spécifique


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

The Ferredoxin/Thioredoxin System of Oxygenic Photosynthesis

Schürmann, Peter ; Buchanan, Bob B.

In: Antioxidants & Redox Signaling, 2008, vol. 10, no. 7, p. 1235-1274

Forty years ago, ferredoxin (Fdx) was shown to activate fructose 1,6-bisphosphatase in illuminated chloroplast preparations, thereby laying the foundation for the field now known as “redox biology.” Enzyme activation was later shown to require the ubiquitous protein thioredoxin (Trx), reduced photosynthetically by Fdx via an enzyme then unknown—ferredoxin:thioredoxin reductase (FTR). These...

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

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...

Université de Neuchâtel

Activation of the Potato Tuber ADP-glucose Pyrophosphorylase by Thioredoxin

Ballicora, Miguel A. ; Frueauf, Jeremiah B. ; Fu, Yingbin ; Schürmann, Peter ; Preiss, Jack

In: The Journal of Biological Chemistry, 2000, vol. 275, no. 2, p. 1315-1320

The potato tuber (Solanum tuberosum L.) ADP-glucose pyrophosphorylase (ADP-GlcPPase) catalyzes the first committed step in starch biosynthesis. The main type of regulation of this enzyme is allosteric, and its activity is controlled by the ratio of activator, 3-phosphoglycerate to inhibitor, Pi. It was reported (Fu, Y., Ballicora, M. A., Leykam, J. F., and Preiss, J. (1998)...

Université de Neuchâtel

A complete ferredoxin/thioredoxin system regulates fundamental processes in amyloplasts

Balmer, Yves ; Vensel, William H. ; Cai, Nick ; Manieri, Wanda ; Schürmann, Peter ; Hurkman, William J. ; Buchanan, Bob B.

In: Proceedings of the National Academy of Sciences of the United States of America (PNAS), 2006, vol. 103, no. 8, p. 2988-2993

A growing number of processes throughout biology are regulated by redox via thiol–disulfide exchange. This mechanism is particularly widespread in plants, where almost 200 proteins have been linked to thioredoxin (Trx), a widely distributed small regulatory disulfide protein. The current study extends regulation by Trx to amyloplasts, organelles prevalent in heterotrophic plant tissues that,...