Articles tagged with Nitrogenases
Researchers at the University of California - San Diego uncovered the 'method of last resort' mechanism used by diazotrophs to protect their nitrogenase enzyme from oxygen damage. This complex process involves a protein called FeSII, which binds to the nitrogenase and halts ammonia production when oxygen levels increase.
Researchers discovered that the iron nitrogenase can convert CO2 into methane and formic acid, making it a promising starting point for developing novel CO2 reductases. The enzyme's low selectivity for CO2 also suggests its potential for widespread use in nature.
Scientists find new partnership between diatoms and Rhizobia bacteria in ocean nitrogen fixation, playing a crucial role in sustaining marine productivity. The discovery has exciting implications for agriculture, particularly for breeding crops that can thrive without fertilizers.
Researchers have identified two essential ferredoxins that play a key role in determining the performance of iron nitrogenase. The discovery opens up new possibilities for elucidating and maximizing nitrogenase's potential, which could lead to sustainable enzymatic production of ammonia and carbon compounds.
Researchers engineer crops and symbiotic bacteria to produce nitrogen fertilizer, reducing reliance on industrially produced fertilizers. The approach aims to create a symbiotic relationship between the bacteria and crop plants, promoting efficient nutrient exchange.
Scientists at the University of California San Diego have taken the first-ever cryo-EM images of nitrogenase during catalytic action, providing new insights into the enzyme's mechanism and its potential for cost-effective and environmentally friendly ammonia production. The atomic-level-resolution images may pave the way for understand...
Researchers at University of Freiburg discover how vanadium-dependent nitrogenase binds two CO molecules simultaneously, enabling reductive process for industrial applications. This breakthrough sheds new light on the mechanistic principles behind nitrogenase's ability to reduce toxic gas carbon monoxide.
A study proposes that the nitrogenase enzyme, essential for photosynthesis, blocked its own activity at 2% atmospheric oxygen levels, stabilizing oxygen levels for nearly two billion years. This negative feedback loop prevented further oxygen production and explains why oxygen levels rose to today's levels.
A newly designed borylene molecule has been found to bind nitrogen at room temperature and normal air pressure, surpassing the capabilities of traditional catalysts like iron and molybdenum. This breakthrough may pave the way for a more energy-efficient method to convert nitrogen into ammonia.
Scientists at Utah State University have identified a new bacterial, iron-only nitrogenase pathway for methane formation, transforming carbon dioxide into methane in a single step. This finding provides a second target for understanding biological methane production and rising emissions.
Researchers uncover an enzymatic pathway in certain microorganisms that produces both ammonia and methane simultaneously. This previously unknown route for natural methane production has significant implications for understanding microbial interactions and the environment.
Researchers from ETH Zurich and Microsoft Research demonstrate that quantum computers can evaluate complex chemical reactions scientifically relevant results. Quantum computers can potentially calculate the reaction mechanism of nitrogenase step by step, but they will serve as a supplement to classical computers.
Researchers at the University of Freiburg have made a significant step towards understanding nitrogenase's function by analyzing its spatial structure. The team discovered that a vanadium ion replaces molybdenum in the enzyme, leading to distinct effects on its geometric and electronic structure.
Researchers found a bacterium can convert CO2 to CO, opening up new avenues for recycling greenhouse gas into biofuels. The discovery establishes nitrogenase enzyme as template for energy-efficient and environmentally-friendly fuel production.
Bacterial nitrogenase produces ammonia by combining atmospheric nitrogen with protons and electrons, moving one electron at a time between symmetrical halves. The enzyme's two-stage engine works efficiently through complex communication between the two halves.
A team of researchers from Utah State University and other institutions found that the two symmetrical halves of nitrogenase work together to regulate electron movements. This cooperative effort allows for more efficient conversion of nitrogen into ammonia, a crucial process for food production and energy development.
Yale University scientists have designed a new chemical compound that mimics the properties of nitrogenase, an enzyme responsible for natural nitrogen fixation. The findings could lead to the development of synthetic catalysts that turn nitrogen into ammonia, reducing transportation and production costs.
Northwestern University scientists have developed a catalyst that can convert nitrogen to ammonia under natural conditions, mimicking the process found in nature.
Scientists used powerful synchrotron spectroscopy and computational modeling to reveal carbon as the mystery atom in nitrogenase, a complex enzyme crucial for life. The research was published online in Science and provides insight into the chemistry of how the cluster behaves, a step toward unraveling its mechanism.
Researchers identified carbon as the key atom in nitrogenase, an enzyme that converts atmospheric nitrogen into a usable form for living things. The discovery could lead to a more efficient and environmentally friendly method for manufacturing fertilizer.
Researchers witness steps in biological nitrogen fixation process, enabling microbes to convert atmospheric nitrogen to nutrients. The study suggests the biological process does not follow the same pathway as the chemical method.