A large proportion of the world's carbon is stored as soil organic matter (SOM). However, the mechanisms regulating the stability of this SOM remain unclear. Recent work suggests that SOM may be stabilized by mechanisms other than chemical recalcitrance. Here, we show that the mineralization rate of starch, a plant polymer commonly found in litter and soil, is concentration dependent, such that its decomposition rate can be reduced by as much as 50% when composing less than approximately 10% of SOM. This pattern is largely driven by low activities of starch-degrading enzymes and low inducibility of enzyme production by microbial decomposers. The same pattern was not observed for cellulose and hemicellulose degradation, possibly because the enzymes targeting these substrates are expressed at constitutively high levels. Nevertheless, given the heterogeneous distribution of SOM constituents, our results suggest a novel low-concentration constraint on SOM decomposition that is independent of chemical recalcitrance. These results may help explain the stability of at least some SOM constituents, especially those that naturally exist in relatively low concentrations in the soil environment.

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The ability of plants and microorganisms to take up organic nitrogen in the form of free amino acids and oligopeptides has received increasing attention over the last two decades, yet the mechanisms for the formation of such compounds in soil environments remain poorly understood. We used Nuclear Magnetic Resonance (NMR) and Electron Paramagnetic Resonance (EPR) spectroscopies to distinguish the reaction of a model protein with a pedogenic oxide (Birnessite, MnO2) from its response to a phyllosilicate (Kaolinite). Our data demonstrate that birnessite fragments the model protein while kaolinite does not, resulting in soluble peptides that would be available to soil biota and confirming the existence of an abiotic pathway for the formation of organic nitrogen compounds for direct uptake by plants and microorganisms. The absence of reduced Mn(II) in the solution suggests that birnessite acts as a catalyst rather than an oxidant in this reaction. NMR and EPR spectroscopies are shown to be valuable tools to observe these reactions and capture the extent of protein transformation together with the extent of mineral response.

Molecular dynamics simulations, conventional and metadynamics, were performed to determine the interaction of model protein Gb1 over kaolinite (001), Na(+)-montmorillonite (001), Ca(2+)-montmorillonite (001), goethite (100), and Na(+)-birnessite (001) mineral surfaces. Gb1, a small (56 residue) protein with a well-characterized solution-state nuclear magnetic resonance (NMR) structure and having α-helix, 4-fold β-sheet, and hydrophobic core features, is used as a model protein to study protein soil mineral interactions and gain insights on structural changes and potential degradation of protein. From our simulations, we observe little change to the hydrated Gb1 structure over the kaolinite, montmorillonite, and goethite surfaces relative to its solvated structure without these mineral surfaces present. Over the Na(+)-birnessite basal surface, however, the Gb1 structure is highly disturbed as a result of interaction with this birnessite surface. Unraveling of the Gb1 β-sheet at specific turns and a partial unraveling of the α-helix is observed over birnessite, which suggests specific vulnerable residue sites for oxidation or hydrolysis possibly leading to fragmentation.

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