Extended conformations of bifurcating electron transfer flavoprotein constitute up to half the population, possibly mediating conformational change.

ABSTRACT: Electron transfer bifurcation enables biological systems to drive unfavourable (endergonic) electron transfer by coupling it to favourable (exergonic) transfer of a second electron. In electron transfer flavoproteins (ETFs), a domain-scale conformational change is believed to sever the favourable pathway after a single electron has used it, thereby preventing the energy dissipation that would accompany exergonic transfer of the second electron. To understand the conformation change that participates in turnover, we have deployed small-angle neutron scattering (SANS) and computational techniques to characterize the bifurcating ETF from Acidaminococcus fermentans (AfeETF). SANS data reveal an overall radius of gyration (R _g) of 30.1 ± 0.2 Å and a maximum dimen

SUBMITTER: Khan SA 

PROVIDER: S-EPMC11536132 | biostudies-literature | 2024 Oct

REPOSITORIES: biostudies-literature