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. Author manuscript; available in PMC: 2013 Jan 8.
Published in final edited form as: Nature. 2009 Mar 19;458(7236):305–309. doi: 10.1038/nature07841

Figure 2.

Figure 2

Left: the spectra of the oxidized (green), reduced (blue), carboxy-ferrous (black) or oxy-ferrous (red) artificial oxygen transport protein 6 with either heme B (A) or heme A as the cofactor (B). These spectra are obtained at -15C where these spectra are stable for more than an hour. Right: stopped-flow spectral changes for mixing the reduced heme B proteins with oxygen at 15C. The fully designed oxygen transport protein 6 (C), shows the transformation of the reduced heme (blue) to the oxy-ferrous state (red) which eventually becomes oxidized (green), while the early intermediate 2 (D) proceeds directly and rapidly to the oxidized form.