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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

    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...