Single-molecule spectroscopy exposes hidden states in an enzymatic electron relay

Iris Grossman (), Haim Yuval Aviram, Gad Armony, Amnon Horovitz, Hagen Hofmann, Gilad Haran and Deborah Fass
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Iris Grossman: Weizmann Institute of Science
Haim Yuval Aviram: Weizmann Institute of Science
Gad Armony: Weizmann Institute of Science
Amnon Horovitz: Weizmann Institute of Science
Hagen Hofmann: Weizmann Institute of Science
Gilad Haran: Weizmann Institute of Science
Deborah Fass: Weizmann Institute of Science

Nature Communications, 2015, vol. 6, issue 1, 1-10

Abstract: Abstract The ability to query enzyme molecules individually is transforming our view of catalytic mechanisms. Quiescin sulfhydryl oxidase (QSOX) is a multidomain catalyst of disulfide-bond formation that relays electrons from substrate cysteines through two redox-active sites to molecular oxygen. The chemical steps in electron transfer have been delineated, but the conformational changes accompanying these steps are poorly characterized. Here we use single-molecule Förster resonance energy transfer (smFRET) to probe QSOX conformation in resting and cycling enzyme populations. We report the discovery of unanticipated roles for conformational changes in QSOX beyond mediating electron transfer between redox-active sites. In particular, a state of the enzyme not previously postulated or experimentally detected is shown to gate, via a conformational transition, the entrance into a sub-cycle within an expanded QSOX kinetic scheme. By tightly constraining mechanistic models, smFRET data can reveal the coupling between conformational and chemical transitions in complex enzymatic cycles.

Date: 2015
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DOI: 10.1038/ncomms9624

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