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...