Site-Differentiated Iron-Sulfur Cluster Ligation Affects Flavin-Based Electron Bifurcation Activity.

ABSTRACT: Electron bifurcation is an elegant mechanism of biological energy conversion that effectively couples three different physiologically relevant substrates. As such, enzymes that perform this function often play critical roles in modulating cellular redox metabolism. One such enzyme is NADH-dependent reduced-ferredoxin: NADP⁺ oxidoreductase (NfnSL), which couples the thermodynamically favorable reduction of NAD⁺ to drive the unfavorable reduction of ferredoxin from NADPH. The interaction of NfnSL with its substrates is constrained to strict stoichiometric conditions, which ensures minimal energy losses from non-productive intramolecular electron transfer reactions. However, the determinants for this are not well understood. One curious feature of NfnSL is that both init

SUBMITTER: Wise CE 

PROVIDER: S-EPMC9503767 | biostudies-literature | 2022 Sep

REPOSITORIES: biostudies-literature