Article
The conserved active-site loop residues of ferrochelatase induce porphyrin conformational changes necessary for catalysis.
Biochemistry - 7 Mar 2006
Shi Zhen, Franco Ricardo, Haddad Raid, Shelnutt John A, Ferreira Gloria C
Abstract excerpt
Binding of porphyrin to murine ferrochelatase, the terminal enzyme of the heme biosynthetic pathway, is investigated by employing a set of variants harboring mutations in a putative porphyrin-binding loop. Using resonance Raman (RR) spectroscopy, the structural properties of the ferrochelatase-bound porphyrins are examined, especially with respect to the porphyrin deformation occurring in the environment of the...
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