2015
DOI: 10.1016/j.molstruc.2014.10.048
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A combined experimental and quantum mechanical investigation on some selected metal complexes of l-serine with first row transition metal cations

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Cited by 6 publications
(2 citation statements)
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“…The tyrosinase-inhibitory effect observed for serine-containing peptides may be because of their capacity to bind copper ions, which are needed for tyrosinase activity. The mechanism of copper binding by serine residues was reported by Mandal et al 47 who found that serine binds to copper ions through the oxygen and nitrogen atoms of its carboxylate and amino groups, respectively.…”
Section: Resultsmentioning
confidence: 90%
See 1 more Smart Citation
“…The tyrosinase-inhibitory effect observed for serine-containing peptides may be because of their capacity to bind copper ions, which are needed for tyrosinase activity. The mechanism of copper binding by serine residues was reported by Mandal et al 47 who found that serine binds to copper ions through the oxygen and nitrogen atoms of its carboxylate and amino groups, respectively.…”
Section: Resultsmentioning
confidence: 90%
“…The tyrosinase-inhibitory effect observed for serine-containing peptides may be because of their capacity to bind copper ions, which are needed for tyrosinase activity. The mechanism of copper binding by serine residues was reported by Mandal et al 47 who found that serine binds to copper ions through the oxygen and nitrogen atoms of its carboxylate and amino groups, respectively. As shown in Table 3, sulfur-containing amino acids (cysteine and methionine) in RBAlbH fractions tend to correlate with tyrosinase-inhibitory and copper-chelating activities (Figure 5a,b).…”
Section: ■ Results and Discussionmentioning
confidence: 90%