|
Figure 5.
Figure 5. (a) Metal insertion into N-MeMP in the presence
and in the absence of enzyme. The relative intensity of mass
spectral signals showing Cu(II) insertion into N-MeMP in
solution in the absence (circles) and in the presence (squares)
of B. subtilis ferrochelatase is shown. Zn(II) insertion in the
presence of ferrochelatase is shown as triangles. (b) Cu(II)
insertion into N-MeMP in the presence of B. subtilis
ferrochelatase mutants H183C (diamonds) and Y13F (triangles),
compared to metallation by the wild-type enzyme (squares).
|
