The active sites of the multiheme
protein cytochrome c nitrite reductase (NiR) and of the copper
enzyme
nitrous oxide reductase (N2OR) have been studied
by
various spectroscopic techniques including continuous wave
multifrequency
and multiquantum electron paramagnetic resonance (EPR), electron spin
echo
envelope modulation (ESEEM), electron nuclear double resonance (ENDOR),
saturation recovery (SATREC), linear electric field effect (LEFE),
magnetic
circular dichroism (MCD), and X-ray absorption spectroscopy
(XAS/EXAFS).
In addition, calculations at the iterative Extended Hueckel and
UHF-INDO/S
level were performed to obtain MO diagrams for the mixed-valence CuA
center in N2OR which help to understand the
unusual
magnetic and electronic properties of this novel chromophore. Based on
the spectroscopic and biochemical properties of both NiR and N2OR,
structural models for their active sites have been developed.