Active-Site Environmental Factors Customize the Photophysics of Photoenzymatic Old Yellow Enzymes

Bryan Kudisch, Daniel Oblinsky, Michael Black, Anna Zieleniewska, Megan Emmanuel, Garry Rumbles, Todd Hyster, Gregory Scholes

Research output: Contribution to journalArticlepeer-review

8 Scopus Citations

Abstract

The development of non-natural photoenzymatic systems has reinvigorated the study of photoinduced electron transfer (ET) within protein active sites, providing new and unique platforms for understanding how biological environments affect photochemical processes. In this work, we use ultrafast spectroscopy to compare the photoinduced electron transfer in known photoenzymes. 12-Oxophytodienoate reductase 1 (OPR1) is compared to Old Yellow Enzyme 1 (OYE1) and morphinone reductase (MR). The latter enzymes are structurally homologous to OPR1. We find that slight differences in the amino acid composition of the active sites of these proteins determine their distinct electron-transfer dynamics. Our work suggests that the inside of a protein active site is a complex/heterogeneous dielectric network where genetically programmed heterogeneity near the site of biological ET can significantly affect the presence and lifetime of various intermediate states. Our work motivates additional tunability of Old Yellow Enzyme active-site reorganization energy and electron-transfer energetics that could be leveraged for photoenzymatic redox approaches.

Original languageAmerican English
Pages (from-to)11236-11249
Number of pages14
JournalJournal of Physical Chemistry B
Volume124
Issue number49
DOIs
StatePublished - 2020

Bibliographical note

Publisher Copyright:
©

NREL Publication Number

  • NREL/JA-5900-77756

Keywords

  • inverted kinetics
  • Old Yellow Enzymes
  • photobiocatalysis
  • photoinduced electron transfer
  • reorganization energy
  • site-directed mutagenesis
  • ultrafast spectroscopy

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