Specific chemical modification explores dynamic structure of the NqrB subunit in Na⁺-pumping NADH-ubiquinone oxidoreductase from Vibrio cholerae.

ABSTRACT: The Na⁺-pumping NADH-ubiquinone oxidoreductase (Na⁺-NQR) is a main ion transporter in many pathogenic bacteria. We previously proposed that N-terminal stretch of the NqrB subunit plays an important role in regulating the ubiquinone reaction at the adjacent NqrA subunit in Vibrio cholerae Na⁺-NQR. However, since approximately three quarters of the stretch (NqrB-Met¹-Pro³⁷) was not modeled in an earlier crystallographic study, its structure and function remain unknown. If we can develop a method that enables pinpoint modification of this stretch by functional chemicals (such as spin probes), it could lead to new ways to investigate the unsettled issues. As the first step to this end, we undertook to specifically attach an alkyne group to

SUBMITTER: Ishikawa M 

PROVIDER: S-EPMC8208467 | biostudies-literature | 2021 Aug

REPOSITORIES: biostudies-literature