Nitrite reductase activity within an antiparallel de novo scaffold.

ABSTRACT: Copper nitrite reductase (CuNiR) is a copper enzyme that converts nitrite to nitric oxide and is an important part of the global nitrogen cycle in bacteria. The relatively simple CuHis₃ binding site of the CuNiR active site has made it an enticing target for small molecule modeling and de novo protein design studies. We have previously reported symmetric CuNiR models within parallel three stranded coiled coil systems, with activities that span a range of three orders of magnitude. In this report, we investigate the same CuHis₃ binding site within an antiparallel three helical bundle scaffold, which allows the design of asymmetric constructs. We determine that a simple CuHis₃ binding site can be designed within this scaffold with enhanced activity relative t

SUBMITTER: Koebke KJ 

PROVIDER: S-EPMC11232943 | biostudies-literature | 2021 Oct

REPOSITORIES: biostudies-literature