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Examines the binding of protoporphyrin IX and metal derivatives to the active site of ferrochelatase using resonance raman spectroscopy. Mechanisms of enzyme catalysis in vivo iron chelation; Formation of low-spin six-coordinate adduct; Distortion of porphyrin substrate.

Nitrous oxide reductase (N[sub2]OR) catalyzes the two-electron reduction of N[sub2]O to N[sub2] and H[sub2]O in the last step of the bacterial denitrification process. It is a dimeric protein. The recently solved crystal structure of N[sub2]OR indicates that in each subunit there is a Cu[subA] center, which is the electron-transfer site, and a Cu[subZ] center, which is the catalytic site. The neighboring Cu[subA] and Cu[subZ] centers are from different subunits. The whole Cu[subZ] cluster is coordinated by seven His ligands with a weakly bound water at the Cu[subI]/Cu[subIV] edge, which is the substrate access site.