Revving up a Designed Copper Nitrite Reductase Using Non-Coded Active Site Ligands.

ABSTRACT: Herein, we report a three stranded coiled-coil (3SCC) de novo protein containing a type II copper center (CuT2) composed of 6-membered ring N-heterocycles. This design yields the most active homogenous copper nitrite reductase (CuNiR) mimic in water. We achieved this result by controlling three factors. First, previous studies with N_δ and N_ε -Methyl Histidine had indicated that a ligand providing pyridine-like electronic character to the copper site was superior to the more donating N_δ for nitrite reduction. By substitution of the parent histidine with the non-coded amino acids pyridyl alanine (3'-Pyridine [3'Py] vs 4'-Pyridine [4'Py]), an authentic pyridine donor was employed without the complications of the coupling of both electronic and tautomeri

SUBMITTER: Pitts WC 

PROVIDER: S-EPMC11329067 | biostudies-literature | 2024 Mar

REPOSITORIES: biostudies-literature