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Modulating proposed electron transfer pathways in P450BM3 led to improved activity and coupling efficiency.

Dominique Darimont1, Martin J Weissenborn2, Bernd A Nebel1

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Engineered P450 enzymes offer electrochemical reduction as an alternative to in vivo methods. Mutating electron transfer pathways significantly boosted NADPH-dependent activity and coupling efficiency in P450BM3 variants.

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Area of Science:

  • Biochemistry
  • Biotechnology
  • Enzyme Engineering

Background:

  • Electrochemical reduction of P450 enzymes is a viable alternative to in vivo applications.
  • Engineered P450BM3 variants with CNT-tags were previously developed for self-assembly on CNT electrodes.
  • While NADPH-dependent activity was enhanced, coupling efficiency remained low in earlier variants.

Purpose of the Study:

  • To investigate the impact of electron transfer pathway (eTP) knockouts on the coupling efficiency of engineered P450BM3 variants.
  • To enhance the activity and coupling efficiency of P450s for electrochemical applications.

Main Methods:

  • Molecular dynamics (MD) simulations were used to identify putative eTPs in P450BM3.
  • Site-directed mutagenesis was employed to create eTP knockout mutants.
  • Enzyme activity and coupling efficiency were measured for both wildtype and mutant P450BM3 variants.

Main Results:

  • Electrically-driven P450 systems showed no improvement with eTP mutations.
  • NADPH-driven P450 systems exhibited a 13-fold increase in activity and a 32-fold increase in coupling efficiency in the most active eTP-mutant.
  • These findings suggest distinct electron transport mechanisms for NADPH reduction versus electrode-mediated reduction.

Conclusions:

  • Mutating specific electron transfer pathways can significantly enhance the performance of NADPH-driven P450BM3 systems.
  • The study provides a tool for improving the coupling and activity of P450 enzymes with non-natural substrates in electrochemical applications.
  • Distinct electron transfer principles are involved in NADPH-dependent reduction and electrode-mediated reduction of P450 enzymes.