Sentences with word «nitrogenase»

«We want to understand the reactions of nitrogenase in order to make the enzyme available for future biotechnological applications.

Both the industrial Haber - Bosch process and natural nitrogenase enzymes use iron (Fe) to catalyze this challenging chemical transformation.

Still, the researchers did not expect that the methane they were seeking would be generated by iron - only nitrogenase in this organism.

The researchers found that the organisms turned on three genes for an enzyme called nitrogenase, which aids nitrogen fixation.

The catalytic center of vanadium nitrogenase: an iron - vanadium cofactor with an unusual carbonate ligand.

The researchers demonstrated for the first time how nitrogenase converts carbon monoxide.

Determining how bacterial nitrogenase works could someday lead to better industrial production of fertilizer

The team's long term goal is to make nitrogenase biotechnologcially useful in order to develop alternatives to industrial chemical processes.

The design proved successful because the compound binds nitrogen from the atmosphere, just as nitrogenase does.

Vanadium nitrogenase found in soil bacteria can in its natural setting perform the same synthesis that is only possible in industrial processes with the aid of extreme pressures and high temperatures.

«Multi-omic Dynamics Associate Oxygenic Photosynthesis with Nitrogenase - mediated H2 production in Cyanothece sp..

«Mechanism of Nitrogenase H2 Formation by Metal - Hydride Protonation Probed by Mediated Electrocatalysis and H / D Isotope Effects.»

At the same time it was known that a variant of nitrogenase containing vanadium rather than molybdenum in its active center and therefore called FeVco can also convert carbon monoxide.

Thus, in addition to the so - called «Haber - Bosch process of nitrogen fixation,» nitrogenase also stimulates a reaction corresponding to the «Fischer - Tropsch synthesis of hydrocarbons,» which can be used on a large scale to synthesize fuels, for instance from industrial waste gases..

Yale chemistry professor Patrick Holland and his team designed a new chemical compound with key properties that help to explain nitrogenase.

«Nitrogenase reacts with nitrogen at a cluster of iron and sulfur atoms, which is strange because other iron - sulfur compounds typically don't react with nitrogen, either in other enzymes or in the thousands of known iron - sulfur compounds synthesized by chemists,» Holland said.

An atomic - resolution structure of a late - stage nitrogenase intermediate reveals nitrogen bound to iron in the active site.

But while nitrogenase is at work, it's also creating something else: dihydrogen (H2).

A team of scientists from Pacific Northwest National Laboratory, Utah State University, Northwestern University, and the University of Utah sought to understand this H2 relaxation mechanism by monitoring the effects of hydrogen (H) vs deuterium (D) on the kinetics of H2 formation when nitrogenase is attached to an electrode.

To make sure this methane - generating pathway was not exclusive to Rhodopseudomonas palustris, they tested for similar abilities in three other nitrogen - fixing bacterial species that have iron - only nitrogenase.

This is where the microbes» nitrogenase enzyme kicks in.

In certain organisms, ammonia is produced from atmospheric nitrogen (N2) by enzymes called nitrogenases.

In nature, only one enzyme — bacterial nitrogenase — can achieve the same reaction, but without emitting excess nitrogen compounds into the environment, or in other words, leaching of nitrates into groundwater.

The program focuses on development of transition - metal complexes that are inspired by the natural photosynthetic enzymes such as nitrogenases, hydrogenases, and the oxygen - evolving complex of photosystem II with the goal of designing catalysts that are chemically stable, active, and highly selective for specific chemical targets.

Einsle's team has already taken a significant step towards greater understanding of nitrogenase.

Within the scope of preparing his doctoral thesis, Daniel Sippel succeeded in producing and crystallizing vanadium nitrogenase.

Nitrogenase, which takes nitrogen in the air and converts it to a biologically useful form by tacking on hydrogens, is among the modelers» most hotly pursued prizes.

Known as the core of nitrogenase, it has been named for the elements it contains.

The research team of Prof. Dr. Oliver Einsle at the University of Freiburg's Institute of Biochemistry has long been exploring the functioning of nitrogenase.

Keeping that in mind, Holland and his team designed a new compound with two distinct properties found in nitrogenase: large shielding groups of atoms that prevented undesired reactions, and a weak iron - sulfur bond that could break easily upon the addition of electrons.

It has been known since 2010 that CO, an inhibitor of Nitrogenase, is slowly converted to hydrocarbons to a minimal extent.

Einsle and his team developed this new crystal structure of the metal core of the nitrogenase.

By applying CO gas to the enzyme during the nitrogenase reaction, the researchers found a binding site for CO and succeeded in documenting the rearrangement.

The enzyme responsible for natural nitrogen fixation is called nitrogenase.

They possess the enzyme nitrogenase, which combines nitrogen with hydrogen to form ammonium.

The reason is that oxygen, a by - product of photosynthesis, poisons the nitrogenase, Bhaya notes.

The bacteria harvest H2 from their PHB store and use their nitrogenase to combine it with nitrogen from the air to make ammonia, the starting material for fertilizer.

Some microbes have evolved proteins called nitrogenases that can split apart nitrogen molecules in the air and weld that nitrogen to hydrogen to make ammonia and other compounds that plants can absorb to get their nitrogen.

Nocera and his colleagues turned to a microbe called Xanthobacter autotrophicus, which naturally harbors a nitrogenase enzyme.

But what is the mechanism for how the nitrogenase active site iron - hydrides relaxed to make this H2?

Nitrogenase will make H2 if run in the absence of N2.

He was among the first to solve the structures of many energy - converting enzymes, including hydrogenases and nitrogenases.

Nitrogenase is central to life on our planet.

Why It Matters: This is an important step toward understanding nitrogenase and how and why the production of H2 is required for its activity.

This work is a critical step toward a mechanistic understanding of the nitrogenase enzyme.

Scientists have known for some time that nitrogenase makes H2 by two different processes.

Summary: To isolate the kinetics of hydrogen production, a team led by Lance Seefeldt, Brian Hoffman, Shelley Minteer, and Simone Raugei used small molecules to quickly shuttle electrons from an electrode to the catalytic half of nitrogenase.

Roughly 10 percent of these nitrogen - fixing microorganisms contain the genetic code for manufacturing a back - up enzyme, called iron iron - only nitrogenase, to do their job.

However, although iron - only nitrogenase was identified several decades ago, scientists had not yet noticed that it, too, could be used by some microorganisms for methane production.