¹H, ¹⁵N and ¹³C backbone resonance assignments of pentaerythritol tetranitrate reductase from Enterobacter cloacae PB2.

ABSTRACT: Pentaerythritol tetranitrate reductase (PETNR) is a flavoenzyme possessing a broad substrate specificity and is a member of the Old Yellow Enzyme family of oxidoreductases. As well as having high potential as an industrial biocatalyst, PETNR is an excellent model system for studying hydrogen transfer reactions. Mechanistic studies performed with PETNR using stopped-flow methods have shown that tunneling contributes towards hydride transfer from the NAD(P)H coenzyme to the flavin mononucleotide (FMN) cofactor and fast protein dynamics have been inferred to facilitate this catalytic step. Herein, we report the near-complete ¹H, ¹⁵N and ¹³C backbone resonance assignments of PETNR in a stoichiometric complex with the FMN cofactor in its native oxidized form, wh

SUBMITTER: Iorgu AI 

PROVIDER: S-EPMC5869876 | biostudies-literature | 2018 Apr

REPOSITORIES: biostudies-literature