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Although the constants for binding of ADP-ribose and NADH to the reduced flavin are similar, and ADP-ribose binds ∼10-fold more strongly when the flavin is oxidized than reduced, whether the oxidation state selectivity and similarity extend to NADH binding to the oxidized flavin (suggesting a binding constant of 25 μM) is unclear.
A protective effect from DA fouling was also observed for other thiol containing substances, thus hinting that the sulfur competes with the amine moiety for the nucleophilic binding to the oxidized catechol, a critical step initiating DA fouling, and therefore reduces the rate of DA polymerization on the electrode surface.
It is difficult to extrapolate from NAD+ binding to the oxidized flavin to NADH binding.
Moreover, N3– and F– are competitive inhibitors of FeSOD, with inhibition constants consistent with their binding to the oxidized state of the enzyme.
Previous spectroscopic studies by our group have revealed that only the Fe(II CDO state is catalytically active, though substrate Cys as well as is its close analogue selenocysteine (Sec) are also capable of binding to the oxidized Fe(III) ion.
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Navab et al. (2012) reported that D-4F accumulates in the intestines regardless of the route of administration; and D-4F harbors a strong binding capacity to oxidized fatty acids such as HETEs and HODEs (Van Lenten et al. 2008).
After binding to proteoglycan, LDL is oxidized, which further activates VSMCs to produce more sulfated proteoglycans and arrest more LDL [ 18].
Thus, similar to the locations of oxidation sensitive methionine residues, the lysine residues that showed significant increases in kDMBNHS between the oxidized and native proteins are located in CN domains involved in Ca2+/CaM binding and stimulation.
GFP STIM1K and its double proline mutant did not show significant increase in binding to Ca2+/CaM upon dialysis under oxidizing conditions.
Nonetheless, the enantioselectivity of TfuDyP also confirms that the observed oxidations are truly enzyme-catalyzed by enantioselective binding of the substrate near the oxidizing heme cofactor.
Previous experiments indicated that Yap1p could discriminate between different sources of oxidative stress but that its DNA-binding properties were independent of the oxidizing agents used [ 4, 41].
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