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

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

On the Quaternary Assembly of Spinach Chloroplast Thioredoxin m

Capitani, Guido ; Schürmann, Peter

In: Photosynthesis Research, 2004, vol. 79, no. 3, p. 281-285

Thioredoxin m from spinach chloroplast has been structurally characterized both by X-ray crystallography and by NMR. Thioredoxin m is known to be monomeric, a finding which is confirmed by the NMR results. The crystal structure of this protein, however, contains two independent molecules per asymmetric unit. This fact was interpreted as contrasting with the NMR results [Neira et al....