Hello Jiri,
I wouldn't choose neither of them, but Co(II). NMR spectroscopists have
been using Co(II) to probe Zn(II) sites in proteins for ages... Check out
Bertini&Luchinat (*DOI: *10.1021/ar00092a002
<https://pubs.acs.org/doi/abs/10.1021/ar00092a002>), or Vallee&Auld (*DOI: *
10.1021/bi00476a001 <https://pubs.acs.org/doi/abs/10.1021/bi00476a001>).
There are many examples of Zn(II) enzymes retaining their activity as
Co(II) surrogates, for instance metallo-beta-lactamases (*DOI: *
10.1021/bi100894r <https://pubs.acs.org/doi/full/10.1021/bi100894r>).
Best wishes,
Javier

On Sun, Jul 29, 2018 at 6:13 PM, chemocev marker <jirivit...@gmail.com>
wrote:

> Dear All
>
> I have a questions about the Zn+2 proteases (Thermolysin based Zn+2 site)
>
> As Zinc is trouble metal when it comes to test the activity.
>
> Which is better substitute for it.
>
> Is MgCl2 or MncCl2
>
> Why one is preferred over the other.
>
> best
>
> Jiri
>
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-- 
Dr. Javier M. González
Instituto de Bionanotecnología del NOA (INBIONATEC-CONICET)
Universidad Nacional de Santiago del Estero (UNSE)
RN9, Km 1125. Villa El Zanjón. (G4206XCP)
Santiago del Estero. Argentina
Tel: +54-(0385)-4238352
Email <bio...@gmail.com> LinkedIn
<https://www.linkedin.com/in/javier-m-gonzalez-inbionatec>

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