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Related Concept Videos

Overview of Nitrogen Metabolism01:20

Overview of Nitrogen Metabolism

8.0K
Nitrogen is a very important element for life because it is a major constituent of proteins and nucleic acids. It is a macronutrient, and in nature, it is recycled from organic compounds and stored in the form of  ammonia, ammonium ions, nitrate, nitrite, or  nitrogen gas by many metabolic processes. Many of these metabolic processes are carried out only by prokaryotes.
The largest pool of nitrogen available in the terrestrial ecosystem is gaseous nitrogen (N2) from the air, but this...
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The Nitrogen Cycle01:49

The Nitrogen Cycle

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Nitrogen atoms, present in all proteins and DNA, are recycled between abiotic and biotic components of the ecosystem. However, the primary form of nitrogen on Earth is nitrogen gas, which cannot be used by most animals and plants. Thus, nitrogen gas must first be converted into a usable form by nitrogen-fixing bacteria before it can be cycled through other living organisms. The use of nitrogen-containing fertilizers and animal waste products in human agriculture has greatly influenced the...
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Structure of Amines01:19

Structure of Amines

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The hybridized nitrogen atom in amines possesses a lone pair of electrons and is bound to three substituents with a bond angle of around 108°, which is less than the tetrahedral angle of 109.5°. However, the C–N–H bond angle is slightly larger at 112°, with a carbon–nitrogen bond length of 147 pm. This carbon–nitrogen bond length of of amines is longer than the carbon–oxygen bond of alcohols (143 pm) but shorter than alkanes’...
2.5K
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Free Energy Changes for Nonstandard States

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The free energy change for a process taking place with reactants and products present under nonstandard conditions (pressures other than 1 bar; concentrations other than 1 M) is related to the standard free energy change according to this equation:
 
where R is the gas constant (8.314 J/K·mol), T is the absolute temperature in kelvin, and Q is the reaction quotient. This equation may be used to predict the spontaneity of a process under any given set of conditions.
Reaction Quotient...
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Chirality at Nitrogen, Phosphorus, and Sulfur

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Chirality is most prevalent in carbon-based tetrahedral compounds, but this important facet of molecular symmetry extends to sp3-hybridized nitrogen, phosphorus and sulfur centers, including trivalent molecules with lone pairs. Here, the lone pair behaves as a functional group in addition to the other three substituents to form an analogous tetrahedral center that can be chiral.
A consequence of chirality is the need for enantiomeric resolution. While this is theoretically possible for all...
5.7K
ATP Synthase: Mechanism01:48

ATP Synthase: Mechanism

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In animals, the mitochondrial F1F0 ATP synthase is the key protein that synthesizes ATP molecules through a complex catalytic mechanism. While the nuclear genome encodes the majority of ATP synthase subunits, the mitochondrial genome encodes some of the enzyme's most critical components. The formation of this multi-subunit enzyme is a complex multi-step process regulated at the level of transcription, translation, and assembly. Defects in one or more of these steps can result in decreased...
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Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase
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Nitrogenase beyond the Resting State: A Structural Perspective.

Rebeccah A Warmack1,2, Douglas C Rees1,2

  • 1Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125, USA.

Molecules (Basel, Switzerland)
|December 23, 2023
PubMed
Summary
This summary is machine-generated.

Nitrogenase enzymes convert nitrogen gas to ammonia using unique iron-sulfur cofactors. Recent studies reveal dynamic enzyme structures and coupled electron-proton transfers crucial for this essential biological process.

Keywords:
cryo-electron microscopyiron–sulfur clustersmetalloenzymesnitrogen fixationnitrogenase

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Area of Science:

  • Biochemistry
  • Enzymology
  • Structural Biology

Background:

  • Nitrogenases catalyze the vital reduction of dinitrogen to ammonia.
  • Understanding the nitrogenase mechanism involves studying substrate binding and cofactor roles.

Purpose of the Study:

  • To review recent experimental characterizations of nitrogenase under turnover conditions.
  • To compare active enzyme forms with resting states and related iron-sulfur clusters.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) for structural determination.
  • Analysis of enzyme dynamics and cofactor interactions.

Main Results:

  • Nitrogenase exhibits obligatory coupling of protein and electron transfers, unlike simpler iron-sulfur clusters.
  • Enzyme and cofactor dynamics are crucial, with homocitrate mediating these changes.
  • Cryo-EM reveals structural asymmetries during turnover, suggesting potential half-of-sites reactivity.

Conclusions:

  • The unique cofactor structure and dynamics are key to nitrogenase function.
  • Coupled electron and proton transfers in nitrogenase are facilitated by specific cofactor features.
  • Further research is needed to establish the mechanistic significance of observed structural asymmetries.