Fig. 3: Iron cofactors in the Hr-like domains of BTSL2 and BTS. | Nature Communications

Fig. 3: Iron cofactors in the Hr-like domains of BTSL2 and BTS.

From: Iron-sensing and redox properties of the hemerythrin-like domains of Arabidopsis BRUTUS and BRUTUS-LIKE2 proteins

Fig. 3

a Diagrams of the MBP fusion proteins of Arabidopsis BTSL2 and BTS N-terminal sequences used for iron quantification and spectroscopy. The E98 and E664 residues of BTSL2 are indicated. b Coomassie-stained SDS-PAGE gel of the indicated purified proteins including the MBP domain (omitted from the labels), 5 µg protein per lane. The results are representative for the number of preparations given in (c). c Quantification of bound iron atoms per polypeptide using the colorimetric chelator Ferene. Values are the mean ± SD of n (in brackets) independent protein purifications. d, e Colour (d) and UV-visible spectra (e) of the as-isolated proteins. The protein concentrations were BTSL2, 462 µM; BTSL2 E98A, 345 µM; BTSL2 E664A, 527 µM; BTS, 222 µM in (d) and diluted as required for UV-visible spectroscopy in (e).

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