RESUMEN
Gamma-ray spectroscopy (GRS) enables continuous estimation of soil water content (SWC) at the subfield scale with a noninvasive sensor. Hydrological applications, including hyper-resolution land surface models and precision agricultural decision making, could benefit greatly from such SWC information, but a gap exists between established theory and accurate estimation of SWC from GRS in the field. In response, we conducted a robust three-year field validation study at a well-instrumented agricultural site in Nebraska, United States. The study involved 27 gravimetric water content sampling campaigns in maize and soybean and 40K specific activity (Bq kg-1) measurements from a stationary GRS sensor. Our analysis showed that the current method for biomass water content correction is appropriate for our maize and soybean field but that the ratio of soil mass attenuation to water mass attenuation used in the theoretical equation must be adjusted to satisfactorily describe the field data. We propose a calibration equation with two free parameters: the theoretical 40K intensity in dry soil and a, which creates an "effective" mass attenuation ratio. Based on statistical analyses of our data set, we recommend calibrating the GRS sensor for SWC estimation using 10 profiles within the footprint and 5 calibration sampling campaigns to achieve a cross-validation root mean square error below 0.035 g g-1.
RESUMEN
A key factor for flavoenzyme activity is the reduction potential of the bound flavin. The reduction potentials of protein-bound flavins span approximately a 500-mV range consistent with flavoenzymes having critical roles in metabolism and a variety of biological processes. Redox potentials of flavoenzymes have traditionally been determined using an electrode-based system with either direct or indirect electrochemical coupling between the protein and the working electrode. An electrode independent method, however, is also now commonly used and involves calculating the unknown flavin reduction potential of the protein from the known reduction potential of a reference or indicator dye. Here, the "classic" potentiometric method and the xanthine/xanthine oxidase methods are described. Both methods rely on equilibrium between protein-bound flavin and redox dyes. The potentiometric method measures the equilibrated redox potential of the protein-dye mixture whereas the xanthine/xanthine oxidase technique relies on slow continuous enzymatic reduction to maintain a constant equilibrium between the protein and the dyes. Because electrochemical equipment is not required, the xanthine/xanthine oxidase method is more accessible and convenient for researchers seeking to determine reduction potentials of flavoproteins or other biological redox centers such as hemes. The xanthine/xanthine oxidase method has been used to determine flavin reduction potentials from +132 to -417mV, demonstrating it is suitable for characterizing the redox properties of most flavoproteins.
