Figure 5 | Scientific Reports

Figure 5

From: Identification of a unique Radical SAM methyltransferase required for the sp3-C-methylation of an arginine residue of methyl-coenzyme M reductase

Figure 5

Characterization of purified methyl-coenzyme M reductase (MCR) from M. acetivorans WWM1 and Mko4551. (a) UV/Vis absorption spectra of purified MCR from the wild type (blue) and the Mko4551 strain (grey), both exhibiting the characteristic features of bound coenzyme F430 at about 423 nm. The spectra were normalised by setting the absorbance at 600 nm to zero. (b) Tm measurement of purified MCR from the wild type (blue) and the Mko4551 strain (grey) with the nanoDSF principle. Upper panel: F330/F350 ratio of the intrinsic tryptophan fluorescence plotted against the temperature, lower panel: Tm calculation by first derivative analysis. Tm (wt) = 82.6 ± 0.2 °C, Tm (ko) = 74.6 ± 0.1 °C. Shown are the curves of four independent measurements for each enzyme. The Tm values are means with standard deviation.

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