PCET Engine

Proton-coupled electron transfer rate prediction from first principles. Validated against 15 benchmark enzyme systems. <4% mean KIE error. SLO-1 KIE within 0.4% of experiment.

📜 Patent Pending — App #64/003,092 Paper Under Review — ACS Omega (ao-2026-03904b)

Why PCET Matters

The Problem

Proton-coupled electron transfer (PCET) is the mechanism behind enzyme catalysis, photosynthesis, respiration, and fuel cells. The kinetic isotope effect (KIE) — how much reaction rates change when hydrogen is replaced by deuterium — reveals the quantum mechanical tunneling contribution.

Predicting KIE accurately requires expensive DFT/QM calculations (hours per system) or empirical fitting. No existing tool provides rapid, general KIE prediction from molecular parameters alone.

The Geometric Approach

Molecular Hessian matrices (force constants) are symmetric positive-definite. The V+/V decomposition separates vibrational mode structure (shape) from coupling strength (magnitude), enabling geometric feature extraction.

This is an entirely novel application of Riemannian geometry to molecular kinetics — zero prior art in the literature. The result: <4% mean KIE error on 15 benchmark enzymes from seconds of computation.

Enzyme Catalysis

Drug design requires understanding how enzymes accelerate reactions. KIE reveals whether proton tunneling is significant.

Energy Conversion

Fuel cells and artificial photosynthesis depend on PCET. Optimizing catalysts requires accurate rate prediction.

Biological Redox

Mitochondrial electron transport, DNA repair, and antioxidant mechanisms all involve PCET chemistry.

Try the API

Benchmark Results

15 enzyme systems with experimentally measured kinetic isotope effects.

<4%

Mean KIE Error

Across 15 benchmark enzymes

15

Enzyme Systems

Validated against experiment

404

Tests Passing

398 core + 6 API tests

KIE vs Tunneling Distance

Kinetic isotope effect scales exponentially with donor-acceptor distance. Hover for enzyme details.

Proton Tunneling Wavefunction

The proton sits in a double-well potential between donor and acceptor. Its quantum wavefunction tunnels through the barrier — heavier deuterium tunnels far less, producing the kinetic isotope effect.

|S₀₀|² (H)

FC overlap

|S₀₀|² (D)

FC overlap

Overlap ratio

H/D ≈ KIE driver

Marcus Free-Energy Surface

Reactant and product free-energy parabolas intersect at the transition state. The proton tunnels below the classical barrier — the shaded region shows the tunneling shortcut.

Ea

Activation energy

Regime

Marcus region

Qcross

Crossing point

Normal Mode Animation — Enzyme Active Site Dynamics

Visualize how vibrational normal modes modulate the donor-acceptor tunneling distance. Select a mode to see how different motions affect proton transfer.

2.70 Å

D-A Distance

C···O separation

0.042

|S₀₀|²

Tunneling probability

D-A Gating

Active Mode

150 cm⁻¹

The donor (C) and acceptor (O) oscillate toward and away from each other, modulating the tunneling distance. This low-frequency gating mode is the primary determinant of proton tunneling rates.

D-A Gating Frequency Correlation

First empirical model predicting donor-acceptor gating from structural features alone. 16 enzyme systems, R² = 0.925.

0.925

Multivariate model fit

−0.938

Pearson r

Ω vs MDA correlation

33

LOO-RMSE (cm−1)

Cross-validated error

Ωgating = 808 − 104 × dDA − 27.5 × MDA

Eliminates need for expensive MD simulations. Predict gating from crystal structure + atom types.

API Playground

Try the PCET Engine live. Toggle to “Live” to hit the real API.

Rate Prediction

Compute PCET rate from molecular parameters. SLO-1 wild-type example.

Enzyme Mutation Screening

Screen mutations with just variant names and measured rates. No crystal structures or QM needed.

Who Uses This

Enzyme Engineering

Screen directed evolution libraries computationally before wet-lab synthesis. Rank 1,000 variants in seconds, synthesize the top 50.

Saves: $50K–$500K per screening round in wet-lab costs

Drug Metabolism

Predict cytochrome P450 PCET rates for drug candidates. Identify metabolic soft spots from molecular parameters, not just binding poses.

Complements: Simcyp, GastroPlus, ADMET tools

Energy & Catalysis

Optimize fuel cell catalysts, electrolyzer electrodes, and industrial biocatalysts. Electrochemical PCET with overpotential-dependent rates.

Markets: Hydrogen, fuel cells, water treatment

Plans

Free

$0
  • ✓ 100 predictions/month
  • ✓ Rate prediction + KIE
  • ✓ Mutation screening (3 variants)
  • ✗ No UQ or batch mode
Most Popular

Professional

$500/mo
  • ✓ 10,000 predictions/month
  • ✓ Mutation screening + saturation scans
  • ✓ Monte Carlo uncertainty quantification
  • ✓ Batch mode + Hessian file input
  • ✓ Per-system calibration
Start Trial

Enterprise

Custom
  • ✓ Unlimited predictions
  • ✓ Dedicated calibration + support
  • ✓ On-prem deployment option
  • ✓ Custom potential surfaces
  • ✓ SLA + priority queue
Contact Us

Consulting: $15K–$50K per enzyme optimization study. We calibrate, screen, and deliver ranked candidates. Learn more

Create Your API Key

Free academic tier: 100 calls/month, single-channel vibronic rates. No credit card required.

Python Usage

Python
import requests

response = requests.post(
    "https://pcet.omnisciences.io/v1/rate/parameters",
    json={
        "donor_acceptor_distance": 2.7,
        "driving_force": -0.2,
        "reorganization_energy": 1.1,
        "coupling": 0.01,
        "temperature": 300,
        "proton_donor_acceptor_distance": 0.95,
        "isotope": "H"
    }
)

data = response.json()
print(f"Rate: {data['rate_constant']:.1f} s⁻¹")
print(f"KIE:  {data['kie_factor']:.1f}")