Copper(II) proteins are amenable for NMR investigations
I. Bertini and R. Pierattelli
Department of Chemistry and Magnetic Resonance Center
(CERM), University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino
Abstract: The possibility of investigating copper proteins by
nuclear magnetic resonance is here treated. It is shown that the solution
structure and dynamic information can be obtained on Type I Cu(II) proteins,
which have a relatively short electron relaxation time (tS
= 10-10 s). The experimental approach,
in this case, is routine, although tailored for fast-relaxing nuclei.
In the case of Type II Cu(II) proteins, when the electron relaxation
times are larger (tS
= 10-8 - 10-9
s) and proton linewidths are broadened beyond detectable limits, heteronuclear
13C spectra with direct detection can
be used and the solution structure can again be obtained.
In this review, it is shown that Cu(II) proteins are now amenable
for NMR investigation, the size being the only limit as in diamagnetic
*Plenary lecture presented at the 2nd Santa Marķa Workshop
on Chemistry Devoted to Bioinorganic Chemistry, Santa Marķa del Mar,
Havana, Cuba, 7-11 July 2003. Other presentations are published in this
issue, pp. 321-388.
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