Periplasmic nitrate reductase (NapA), a member of the DMSO reductase, catalyze the reduction of nitrate (NO3-) to nitrite (NO2-). The catalytic reaction occurs at the Mo-center, where two pyranopterin cofactors coordinate Mo. Two pterins are designated as the P- and D-pterins. The P-pterin is proximal to the [4Fe4S] cluster, while the D-pterin is distal to the [4Fe4S] cluster and oriented towards the interior of the protein. P-pterin is involved in electron transfer, and D-pterin is involved in tuning the redox potential. In Campylobacter jejuni NapA, we have identified several residues that stabilize the pterin cofactor through H-bonding or p-stacking. We have mutated these residues and conducted steady-state kinetic studies on these variants. The results of these studies will be discussed in the context of pterin conformation and enzyme function.

Evaluating the effects of pyran ring scission on the kinetics of periplasmic nitrate reductase of Campylobacter jejuni

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