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Evaluating apoenzyme–coenzyme–substrate interactions of methane monooxygenase with an engineered active site for electron harvesting: a computational study

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Abstract

Low-temperature methane oxidation is one of the greatest challenges in energy research. Although methane monooxygenase (MMO) does this catalysis naturally, how to use this biocatalyst in a fuel cell environment where the electrons generated during the oxidation process is harvested and used for energy generation has not yet been investigated. A key requirement to use this enzyme in a fuel cell is wiring of the active site of the enzyme directly to the supporting electrode. In soluble MMO (sMMO), two cofactors, i.e., nicotinamide adenine di-nucleotide (NAD+) and flavin adenine dinucleotide (FAD) provide opportunities for direct attachment of the enzyme system to a supporting electrode. However, once modified to be compatible with a supporting metal electrode via FeS functionalization, how the two cofactors respond to complex binding phenomena is not yet understood. Using docking and molecular dynamic simulations, modified cofactors interactions with sMMO-reductase (sMMOR) were studied. Studies revealed that FAD modification with FeS did not interfere with binding phenomena. In fact, FeS introduction significantly improved the binding affinity of FAD and NAD+ on sMMOR. The simulations revealed a clear thermodynamically more favorable electron transport path for the enzyme system. This system can be used as a fuel cell and we can use FeS-modified-FAD as the anchoring molecule as opposed to using NAD+. The overall analysis suggests the strong possibility of building a fuel cell that could catalyze methane oxidation using sMMO as the anode biocatalyst.

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Authors and Affiliations

  1. Biological and Agricultural Engineering Department, Texas A&M University, College Station, TX, USA

    Sikai Zhang, Raghupathy Karthikeyan & Sandun D. Fernando

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  1. Sikai Zhang
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  2. Raghupathy Karthikeyan
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  3. Sandun D. Fernando
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Correspondence to Sandun D. Fernando.

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Zhang, S., Karthikeyan, R. & Fernando, S.D. Evaluating apoenzyme–coenzyme–substrate interactions of methane monooxygenase with an engineered active site for electron harvesting: a computational study. J Mol Model 24, 347 (2018). https://doi.org/10.1007/s00894-018-3876-4

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  • DOI: https://doi.org/10.1007/s00894-018-3876-4

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