Nitrogenase

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Nitrogenase

Nitrogenase (pronunciation: /ˌnaɪˈtrɒdʒɪneɪz/) is an enzyme that plays a crucial role in the biological nitrogen fixation process. It is responsible for the reduction of atmospheric nitrogen (N2) to ammonia (NH3).

Etymology

The term "Nitrogenase" is derived from the element "Nitrogen" and the suffix "-ase" which is used in biochemistry to form names of enzymes.

Function

Nitrogenase is a complex enzyme system that is found in certain bacteria, known as diazotrophs. These bacteria have the unique ability to convert atmospheric nitrogen into a form that can be used by plants. The enzyme catalyzes the conversion of nitrogen (N2) to ammonia (NH3), a process known as nitrogen fixation. This process is vital for life because it provides a form of nitrogen that can be used to synthesize amino acids and nucleotides, the building blocks of proteins and DNA, respectively.

Structure

Nitrogenase is composed of two proteins: an iron protein and a molybdenum-iron protein. The iron protein, also known as the Fe protein or nitrogenase reductase, is a homodimer with an ATP-binding site and a [4Fe-4S] cluster. The molybdenum-iron protein, also known as the MoFe protein, contains a P-cluster and a FeMo-cofactor, which is the site of nitrogen reduction.

Related Terms

  • Biological nitrogen fixation: The process by which atmospheric nitrogen is converted into a usable form by certain types of bacteria.
  • Diazotrophs: Bacteria that can fix nitrogen.
  • Enzyme: A protein that acts as a biological catalyst.
  • Ammonia: A compound of nitrogen and hydrogen, which is a product of nitrogen fixation.

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