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Abstract While it has been known for some time that reducing fluids have bleached red beds adjacent to fault zones and regionally across the Colorado Plateau, the volumes of fluids expelled along faults have never been quantified. We have developed and applied a suite of one-dimensional hydrologic models to test the hypothesis that internally generated, reducing fluids migrated up sub-basin bounding faults across the Paradox Basin and bleached overlying red beds. The internal fluid driving mechanisms included are mechanical compaction, petroleum and natural gas generation, aquathermal expansion of water, and clay dewatering. The model was calibrated using pressure, temperature, porosity, permeability, and vitrinite reflectance data. Model results indicate that sediment compaction was the most important pressure generation mechanism, producing the majority of internal fluids sourced during basin evolution. Peak fluid migration occurred during the Pennsylvanian–Permian (325–300 Ma) and Cretaceous (95–65 Ma) periods, the latter being concurrent with simulated peak oil/gas generation (87–74 Ma), which likely played a role in the bleaching of red beds. Batch geochemical advection models and mass balance calculations were utilized to estimate the volume of bleaching in an idealized reservoir having a thickness (~100 m) and porosity (0.2) corresponding to bleached reservoirs observed in the Paradox Basin. Bleaching volume calculations show that internal fluid driving mechanisms were likely responsible for fault-related alteration observed within the Wingate, Morrison, and Navajo Formations in four localities across the Paradox Basin in the Colorado Plateau, Utah and Colorado, USA. The volume calculation required that 33%–55% of the total basinal fluids, composed of hydrogen-sulfide and paleo-seawater, migrated into an overlying red bed reservoir (0.5 wt% Fe2O3). 

Dynemicin is an enediyne natural product fromMicromonospora chersinaATCC53710. Access to the biosynthetic gene cluster of dynemicin has enabled thein vitrostudy of gene products within the cluster to decipher their roles in assembling this unique molecule. This paper reports the crystal structure of DynF, the gene product of one of the genes within the biosynthetic gene cluster of dynemicin. DynF is revealed to be a dimeric eight-stranded β-barrel structure with palmitic acid bound within a cavity. The presence of palmitic acid suggests that DynF may be involved in binding the precursor polyene heptaene, which is central to the synthesis of the ten-membered ring of the enediyne core.