Cu(II) complex formation by ACES buffer.

Cu(II) complex formation by ACES buffer.
J Inorg Biochem. 2013 Sep 6;129C:58-61
Authors: Zawisza I, Rózga M, Poznański J, Bal W
Abstract
ACES (N-(2-Acetamido)-2-aminoethanesulfonic acid), a popular Good's buffer, binds Cu(II) ions with a moderate affinity. Although this interaction was the subject of previous studies, no consensus in the literature was found. We used potentiometry to establish binding constants, and controlled the potentiometric model selection and binding constant calculations by UV-vis spectroscopy. As a result, we obtained a consistent set of complex stoichiometries and binding constants in this system, which contains Cu(2+), CuL(+), CuL2, CuH-1L2(-1) and CuH(-)2L2(-2) complexes. The negative indexes at H atoms in these formulae denote the Cu(II) assisted deprotonation of the amide nitrogen present in the ACES molecule. The affinity of ACES for Cu(II) strongly depends on the concentration and ACES:Cu(II) ratio, reaching submicromolar apparent affinities at ratios higher than 100. These results will enable more accurate determinations of biologically relevant stability constants of Cu(II) complexes using ACES buffer.
PMID: 24077022 [PubMed - as supplied by publisher]

Source: Journal of Inorganic Biochemistry - September 6, 2013 Category: Biochemistry Authors: Zawisza I, Rózga M, Poznański J, Bal W Tags: J Inorg Biochem Source Type: research