Cycling Phosphorus and Nitrogen through Cropping Systems in an Intensive Dairy Production Region

As pressure on the dairy industry to reduce its environmental impact increases, efficient recycling of manure nutrients through local cropping systems becomes crucial. The aim of this study was to calculate annual nitrogen (N) and phosphorus (P) budgets in six counties located in the Magic Valley, Idaho and estimate what distance manure would need to be transported to be in balance with crop nutrient demand given current dairy cattle populations and cropping systems. Our analysis suggests that crop N needs will not be met solely by manure, and synthetic fertilizer will need to be applied. However, to balance P with crop production, manure would need to be transported a minimum of 12.9 km from dairies and would have to replace synthetic fertilizer P on 91% of regional cropland. Education of producers and technical specialists would be necessary to improve the management of manure use in regional cropping systems. Technical solutions such as alternative diets for cattle and nutrient capture from manure streams will also likely be necessary to bring regional P into balance to protect environmental quality and improve the sustainability of the regional dairy industry

Structural adaptations of photosynthetic complex I enable ferredoxin-dependent electron transfer.

Photosynthetic complex I enables cyclic electron flow around photosystem I, a regulatory mechanism for photosynthetic energy conversion. We report a 3.3-A resolution cryo-EM structure of photosynthetic complex I from the cyanobacterium Thermosynechococcus elongatus. The model reveals structural adaptations that facilitate binding and electron transfer from the photosynthetic electron carrier ferredoxin. By mimicking cyclic electron flow with isolated components in vitro, we demonstrate that ferredoxin directly mediates electron transfer between photosystem I and complex I, instead of using intermediates such as NADPH. A large rate constant for association of ferredoxin to complex I indicates efficient recognition, with the protein subunit NdhS being the key component in this process. Copyright © 2018, American Association for the Advancement of Science