Kinetic studies reveal a key role of a redox-active glutaredoxin in the evolution of the thiol-redox metabolism of trypanosomatid parasites.

ABSTRACT: Trypanosomes are flagellated protozoan parasites (kinetoplastids) that have a unique redox metabolism based on the small dithiol trypanothione (T(SH)₂). Although GSH may still play a biological role in trypanosomatid parasites beyond being a building block of T(SH)₂, most of its functions are replaced by T(SH)₂ in these organisms. Consequently, trypanosomes have several enzymes adapted to using T(SH)₂ instead of GSH, including the glutaredoxins (Grxs). However, the mechanistic basis of Grx specificity for T(SH)₂ is unknown. Here, we combined fast-kinetic and biophysical approaches, including NMR, MS, and fluorescent tagging, to study the redox function of Grx1, the only cytosolic redox-active Grx in trypanosomes. We observed that Grx1

SUBMITTER: Manta B 

PROVIDER: S-EPMC6398122 | biostudies-literature | 2019 Mar

REPOSITORIES: biostudies-literature