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. 2013 Mar 7;42(9):3088-91.
doi: 10.1039/c2dt32018e. Epub 2012 Dec 3.

Human ferredoxin-2 displays a unique conformational change

Wenbin Qi  1 , Jingwei Li, J A Cowan
Affiliations

Human ferredoxin-2 displays a unique conformational change

Wenbin Qi et al. Dalton Trans. .

Abstract

Human ferredoxin-1 (hFd1) and human ferredoxin-2 (hFd2) share high sequence similarity but serve on distinct cellular pathways. A unique conformational change is observed when holo hFd2 is warmed to physiological temperatures, or higher. Enzymatic studies show that this conformational change causes the increase of affinity between hFd2 and adrenodoxin reductase. No such change was observed for hFd1, which may contribute to the distinct cellular functions of hFd1 and hFd2 under physiological conditions.

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Figures

Figure 1
Figure 1
Change in 414 nm absorbance following warming of holo hFd1 (A) and holo hFd2 (B). Inset graphs show the change of absorbance at 414 nm with increasing temperature. These points are taken at discrete time intervals and do not represent thermodynamic equilibria. In fact an increase in absorbance to a common plateau is observed even at lower temperatures (including 37 C), but take longer to reach that equilibrium point (Figure 2) reflecting slower transition times at lower temperature.
Figure 2
Figure 2
Rate of heating-induced conformational change increases with higher incubation temperatures for holo hFd2.
Figure 3
Figure 3
Comparison of the absorbance change during a heating and cooling cycle for hFd1 (Red) and hFd2 (Green).
Figure 4
Figure 4
CD signal from the cluster center when holo hFd2 is incubated up to 55 C (blue trace).
Figure 5
Figure 5
Comparison of chemical shift perturbations for hFd1 and hFd2 after heating to 55 C. Chemical shift changes of amide proton and nitrogen signals, and Δδavg are shown for all comparable residues. The x-axes have been systematically numbered clockwise, as observed from the 2-D spectra, since the hFd2 residues have not been assigned
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