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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

Oxidation-Reduction Properties of Chloroplast Thioredoxins, Ferredoxin:Thioredoxin Reductase, and Thioredoxin f-Regulated Enzymes

Hirasawa, Masakazu ; Schürmann, Peter ; Jacquot, Jean-Pierre ; Manieri, Wanda ; Jacquot, Pierre ; Keryer, Eliane ; Hartman, Fred C. ; Knaff, David B.

In: Biochemistry, 1999, vol. 38, no. 16, p. 5200-5205

Oxidation-reduction midpoint potentials were determined, as a function of pH, for the disulfide/dithiol couples of spinach and pea thioredoxins f, for spinach and Chlamydomonas reinhardtii thioredoxins m, for spinach ferredoxin:thioredoxin reductase (FTR), and for two enzymes regulated by thioredoxin f, spinach phosphoribulokinase (PRK) and the...

Université de Neuchâtel

Oxidation−Reduction and Activation Properties of Chloroplast Fructose 1,6-Bisphosphatase with Mutated Regulatory Site

Balmer, Yves ; Stritt-Etter, Anne-Lise ; Hirasawa, Masakazu ; Jacquot, Jean-Pierre ; Keryer, Eliane ; Knaff, David B. ; Schürmann, Peter

In: Biochemistry, 2001, vol. 40, no. 50, p. 15444–15450

The concentration of Mg2+ required for optimal activity of chloroplast fructose 1,6-bisphosphatase (FBPase) decreases when a disulfide, located on a flexible loop containing three conserved cysteines, is reduced by the ferredoxin/thioredoxin system. Mutation of either one of two regulatory cysteines in this loop (Cys155 and Cys174 in spinach FBPase) produces an enzyme with a...

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

Redox Signaling in Chloroplasts : Cleavage of Disulfides by an Iron-Sulfur Cluster

Dai, Shaodong ; Schwendtmayer Cristina ; Schürmann, Peter ; Ramaswamy, S ; Eklund, Hans

In: Science, 2000, vol. 287, no. 5453, p. 655-658

Light generates reducing equivalents in chloroplasts that are used not only for carbon reduction, but also for the regulation of the activity of chloroplast enzymes by reduction of regulatory disulfides via the ferredoxin:thioredoxin reductase (FTR) system. FTR, the key electron/thiol transducer enzyme in this pathway, is unique in that it can reduce disulfides by an iron-sulfur cluster, a...

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...

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1 Schurmann, P