Partial Co(II) substitution in the three-zinc site of P. citrinum nuclease P1 has been achieved. The Co(II) ion is found to bind to the site of the most EDTA-labile Zn atom with an 80% site occupancy. An affinity constant of 10(5) M(-1) for metal binding was determined from the visible spectra which also indicate a six-coordinate Co(II) geometry. The hyperfine-shifted H-1 NMR resonances suggest that metal substitution occurred at the Zn3 site (X-ray atom numbering).
POLYMETALLIC HYDROLYTIC ZINC ENZYMES - PROBING THE SITE OF NUCLEASE P1 THROUGH COBALT(II) SUBSTITUTION / Ferretti, S; Luchinat, C; Sola, Marco; Battistuzzi, Gianantonio. - In: INORGANICA CHIMICA ACTA. - ISSN 0020-1693. - STAMPA. - 234:(1995), pp. 9-11.
POLYMETALLIC HYDROLYTIC ZINC ENZYMES - PROBING THE SITE OF NUCLEASE P1 THROUGH COBALT(II) SUBSTITUTION
SOLA, Marco;BATTISTUZZI, Gianantonio
1995
Abstract
Partial Co(II) substitution in the three-zinc site of P. citrinum nuclease P1 has been achieved. The Co(II) ion is found to bind to the site of the most EDTA-labile Zn atom with an 80% site occupancy. An affinity constant of 10(5) M(-1) for metal binding was determined from the visible spectra which also indicate a six-coordinate Co(II) geometry. The hyperfine-shifted H-1 NMR resonances suggest that metal substitution occurred at the Zn3 site (X-ray atom numbering).
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