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To view the distinctive spectrum activity of oxy-Hb, the oxy-Hb must be scanned in (500700 nm) wavelength before adding the iron or chelators to analyze their influence on oxyhemoglobin spectra, oxy-Hb has two distinct peaks at 541 and 577 nm

Structural comparison of the GSH-bound OsDHAR and GSH-bound OaGST structures revealed that the binding position of GSH is very similar to the H-site binding, although the residues involved in the H-site binding of GSH are very different from each other

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