ArticleChemistry (Weinheim an der Bergstrasse, Germany)2019
Increase of Redox Potential during the Evolution of Enzymes Degrading Recalcitrant Lignin.
Article in Chemistry (Weinheim an der Bergstrasse, Germany), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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13 citing papers in PubMed.
- Understanding Lignin Oxidation by a Two-Domain Multicopper Oxidase fromBiochemistry · 2026Article
- Directed evolution of APOX for proximity labeling using phenols with high redox potentials.Cell chemical biology · 2026Article
- Fluctuation Relations to Calculate Protein Redox Potentials from Molecular Dynamics Simulations.Journal of chemical theory and computation · 2024Article
- Recent Theoretical Insights into the Oxidative Degradation of Biopolymers and Plastics by Metalloenzymes.International journal of molecular sciences · 2023Review
- Article
- Ancestral sequence reconstruction as a tool to study the evolution of wood decaying fungi.Frontiers in fungal biology · 2022Review
- Agaricales Mushroom Lignin Peroxidase: From Structure-Function to Degradative Capabilities.Antioxidants (Basel, Switzerland) · 2021Article
- Setting the stage for evolution of a new enzyme.Current opinion in structural biology · 2021Review
- Mutational and structural analysis of an ancestral fungal dye-decolorizing peroxidase.The FEBS journal · 2021Article
- Experimental and theoretical insights into the effects of pH on catalysis of bond-cleavage by the lignin peroxidase isozyme H8 from Phanerochaete chrysosporium.Biotechnology for biofuels · 2021Article
- Comparing Ligninolytic Capabilities of Bacterial and Fungal Dye-Decolorizing Peroxidases and Class-II Peroxidase-Catalases.International journal of molecular sciences · 2021Article
- Peroxidase evolution in white-rot fungi follows wood lignin evolution in plants.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Increase of Redox Potential during the Evolution of Enzymes Degrading Recalcitrant Lignin.Chemistry (Weinheim an der Bergstrasse, Germany) · 2019Article
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5 authors.
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Abstract
To investigate how ligninolytic peroxidases acquired the uniquely high redox potential they show today, their ancestors were resurrected and characterized. Unfortunately, the transient Compounds I (CI) and II (CII) from peroxide activation of the enzyme resting state (RS) are unstable. Therefore, the reduction potentials (E°') of the three redox couples (CI/RS, CI/CII and CII/RS) were estimated (for the first time in a ligninolytic peroxidase) from equilibrium concentrations analyzed by stopped-flow UV/Vis spectroscopy. Interestingly, the E°' of rate-limiting CII reduction to RS increased 70 mV from the common peroxidase ancestor to extant lignin peroxidase (LiP), and the same boost was observed for CI/RS and CI/CII, albeit with higher E°' values. A straightforward correlation was found between the E°' value and the progressive displacement of the proximal histidine Hϵ1 chemical shift in the NMR spectra, due to the higher paramagnetic effect of the heme Fe
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