Nitrogen Fixation and Hydrogen Evolution by Sterically Encumbered Mo-Nitrogenase.

ABSTRACT: The substrate-reducing proteins of all nitrogenases (MoFe, VFe, and FeFe) are organized as α₂ß₂(γ₂) multimers with two functional halves. While their dimeric organization could afford improved structural stability of nitrogenases in vivo, previous research has proposed both negative and positive cooperativity contributions with respect to enzymatic activity. Here, a 1.4 kDa peptide was covalently introduced in the proximity of the P cluster, corresponding to the Fe protein docking position. The Strep-tag carried by the added peptide simultaneously sterically inhibits electron delivery to the MoFe protein and allows the isolation of partially inhibited MoFe proteins (where the half-inhibited MoFe protein was targeted). We confirm that the partially fu

SUBMITTER: Cadoux C 

PROVIDER: S-EPMC10207099 | biostudies-literature | 2023 May

REPOSITORIES: biostudies-literature