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\begin{document}

\title{Histidine protonation states are key in the LigI catalytic reaction
mechanism}



\author[1]{LINA ZHAO}%
\author[2]{Dibyendu Mondal}%
\author[3]{Weifeng Li}%
\author[4]{Yuguang Mu}%
\author[1]{Philipp Kaldis}%
\affil[1]{Lund University}%
\affil[2]{University of California San Francisco}%
\affil[3]{Shandong University}%
\affil[4]{Nanyang Technological University}%


\vspace{-1em}



  
  \date{May 04, 2024}


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\begin{abstract}
Lignin is one of the world's most abundant organic polymers, and
2-pyrone-4,6-dicarboxylate lactonase (LigI) catalyzes the hydrolysis of
2-pyrone-4,6-dicarboxylate (PDC) in the degradation of lignin. The pH
has profound effects on enzyme catalysis and therefore we studied this
in the context of LigI. We found that changes of the pH mostly affects
surface residues, while the residues at the active site are more subject
to changes of the surrounding microenvironment. In accordance with this,
a high pH facilitates the deprotonation of the substrate. Detailed free
energy calculations by the empirical valence bond (EVB) approach
revealed that the overall hydrolysis reaction is more likely when the
three active site histidines (His31, His33 and His180) are protonated at
the e \selectlanguage{english}site, however, protonation at the \selectlanguage{greek}δ \selectlanguage{english}site may be favored during
specific steps of reaction. Our studies have uncovered the determinant
role of the protonation state of the active site residues His31, His33
and His180 in the hydrolysis of PDC.%
\end{abstract}%



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