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Figure 1
(a) The covalent modification of the LTQ cofactor of LOXL2 by 2HP. After the tautomerization of the hydrazone to the azo form, LTQ-2HP ligates to the active site Cu2+. The 2HP-modified LTQ (LTQ-2HP) containing the peptide was detected by mass spectrometry (Meier, Go, et al., 2022BB13). Based on the close resemblances of UV–vis and resonance Raman spectra of 2HP-inhibited LOXL2 and the model compound 2, we hypothesize that LTQ-2HP serves as a tridentate ligand to the active site CuII in LOXL2 (Meier, Moon et al., 2022BB15). The +2 charge of CuII is expected to be canceled out by the 4-oxoanion of LTQ-2HP and a nearby acidic residue or a water mol­ecule (Meier, Kuczera et al., 2022BB14). (b) During the recrystallization of the dark red solids (2) isolated from an equimolar mixture of the LTQ-2HP model compound (1) and CuCl2(phen) in anhydrous methanol, we first isolated dark-red crystals (3), then also isolated (4) from the mother liquor that was left for a week at room temperature.

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ISSN: 2056-9890
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