Current agricultural productivity depends on an exogenous nutrient supply to crops. This is of special relevance in cereal production, a fundamental part of the trophic chain that plays a vital role in the human diet. However, our agricultural practices entail highly detrimental side-effects from an environmental point of view. Long-term nitrogen fertilization in croplands results in degradation of soil, water, and air quality, producing eutrophication and subsequently contributing to global warming. In accordance with this, there is a biotechnological interest in using nitrogen-fixing microorganisms to enhance crop growth without adding chemically synthesized nitrogen fertilizers. This is particularly beneficial in paddy fields, where about 60% of the synthetic fertilizer that has been applied is dissolved in the water and washed away. In these agricultural systems, N2-fixing cyanobacteria show a promising biotechnological potential as biofertilizers, improving soil fertility while reducing the environmental impact of the agricultural practice. In the current study, Andalusian paddy fields have been explored to isolate N2-fixing cyanobacteria. These endogenous microorganisms have been subsequently re-introduced in a field trial in order to enhance rice production. Our results provide valuable insights regarding the use of an alternative natural source of nitrogen for rice production.

Cytochrome cM was first described in 1994 and its sequence has been found in the genome of manifold cyanobacterial species ever since. Numerous studies have been carried out with the purpose of determining its function, but none of them has given place to conclusive results so far. Many of these studies are based on the assumption that cytochrome cM is a soluble protein located in the thylakoid lumen of cyanobacteria. In this work, we have reevaluated the sequence of cytochrome cM, with our results showing that its most probable 3D structure is strongly similar to that of the C subunit of the bacterial nitric oxide reductase. The potential presence of an α-helix tail, which could locate this protein in the thylakoid membrane, further supports this hypothesis, thus providing a new, unexpected role for this redox protein.