Strong Electron Correlation in Nitrogenase Cofactor, FeMoco

TL;DR

This study investigates the electronic structure of the nitrogenase cofactor FeMoco, emphasizing the importance of strong electron correlation and determining the minimal active space needed for accurate multireference descriptions.

Contribution

It systematically explores active-space sizes for capturing strong correlation in FeMoco and related moieties using advanced wavefunction methods, providing insights into electronic structure modeling.

Findings

Larger active spaces are necessary for a consistent multireference solution.

Smaller active spaces show a competition between single-reference and multireference solutions.

Fractional natural-orbital occupations effectively assess electron correlation levels.

Abstract

FeMoco, MoFe$_7$S$_9$C, has been shown to be the active catalytic site for the reduction of nitrogen to ammonia in the nitrogenase protein. An understanding of its electronic structure including strong electron correlation is key to designing mimic catalysts capable of ambient nitrogen fixation. Active spaces ranging from [54, 54] to [65, 57] have been predicted for a quantitative description of FeMoco's electronic structure. However, a wavefunction approach for a singlet state using a [54,54] active space would require 10$^{29}$ variables. In this work, we systematically explore the active-space size necessary to qualitatively capture strong correlation in FeMoco and two related moieties, MoFe$_3$S$_7$ and Fe$_4$S$_7$. Using CASSCF and 2-RDM methods, we consider active-space sizes up to [14,14] and [30,30], respectively, with STO-3G, 3-21G, and DZP basis sets and use fractional natural-orbital occupation numbers to assess the level of multireference electron correlation, an examination of which reveals a competition between single-reference and multi-reference solutions to the electronic Schr\"{o}dinger equation for smaller active spaces and a consistent multi-reference solution for larger active spaces.