Zinc-sulfur bonds of aspartate transcarbamylase studied by x-ray absorption spectroscopy.
X-ray absorption spectra have been recorded for aspartate transcarbamylase [unligated and ligated with the transition-state analogue N-(phosphonoacetyl)-L-aspartate] and for the model compound zinc dimethyldithiocarbamate. The spectra confirm that, in the enzyme, the zinc atom is ligated to four sulfur atoms, with a mean distance of 2.34 +/- 0.03 A. A spread in bond lengths of 0.1 +/- 0.03 A is possible, due to thermal and/or static disorder. No significant difference was found between the spectra of the ligated and unligated enzymes.
D001221:Aspartate Carbamoyltransferase; D004926:Escherichia coli / Q000201:enzymology; D013057:Spectrum Analysis; D013455:Sulfur; D014965:X-Rays; D015032:Zinc
D013455:Sulfur; D001221:Aspartate Carbamoyltransferase; D015032:Zinc