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FEMOCO

FeMoco

Cofactor of nitrogenase

FeMoco (FeMo cofactor) or M-cluster is the primary cofactor of nitrogenase. Nitrogenase is the enzyme that catalyzes the conversion of atmospheric nitrogen

FeMoco

Molybdenum

Chemical element with atomic number 42 (Mo)

nitrogen fixation. Most nitrogenases contain an iron–molybdenum cofactor FeMoco, which is believed to contain either Mo(III) or Mo(IV). By contrast Mo(VI)

Molybdenum

Carbon

Chemical element with atomic number 6 (C)

of an otherwise labile species. In nature, the iron-molybdenum cofactor (FeMoco) responsible for microbial nitrogen fixation likewise has an octahedral

Carbon

Molybdenum in biology

Use of molybdenum by organisms

molybdenum cofactor. The only known exception is nitrogenase, which uses the FeMoco cofactor, which has the formula Fe7MoS9C. In terms of function, molybdoenzymes

Molybdenum in biology

Molybdenum_in_biology

Serena DeBeer

American-born chemist

different forms of nitrogenase enzymes with FeMoco and FeVco active sites, Selenium-incorporated FeMoco, as well as spectroscopic characterization of

Serena DeBeer

Serena_DeBeer

Bioinorganic chemistry

Study of the role of metals in biology

intermediates. Bioorganometallic enzymes and proteins include the hydrogenases, FeMoco in nitrogenase, and methylcobalamin. These naturally occurring organometallic

Bioinorganic chemistry

Bioinorganic_chemistry

Nitrogen fixation

Conversion of dinitrogen into ammonia

FeMoco, an abbreviation for the iron-molybdenum cofactor. The mechanism proceeds via a series of protonation and reduction steps wherein the FeMoco active

Nitrogen fixation

Nitrogen_fixation

Threshold theorem

Quantum error correction schemes can suppress the logical error rate arbitrarily low

discovery, energy production, climate modeling and fertilizer production (e.g. FeMoco) as well. Because of this, quantum computers may be better than classical

Threshold theorem

Threshold_theorem

Iron–sulfur cluster

Molecular structures and ubiquitous inorganic cofactors found in all domains of life

chemistry Ligand (biochemistry) Iron-binding proteins Biometal (biology) FeMoco Axel Kern; Christian Näther; Felix Studt; Felix Tuczek (2004). "Application

Iron–sulfur cluster

Iron–sulfur_cluster

Azotobacter vinelandii

Species of bacterium

states. The enzyme possesses molybdenum iron-sulfido cluster cofactors (FeMoco) as active sites, each bearing two pseudocubic iron-sulfido structures.

Azotobacter vinelandii

Azotobacter_vinelandii

Protochlorophyllide reductase

protochlorophyllide-bound active site (which, distinct from nitrogenase, does not contain FeMoco). The reduction requires significantly less input than the nitrogenase reaction

Protochlorophyllide reductase

Protochlorophyllide_reductase

Bioorganometallic chemistry

Study of biologically active molecules that contain carbon-metal bonds

of a nickel–methyl bond in cofactor F430. The iron–molybdenum cofactor (FeMoco) of nitrogenases contains an Fe6C unit and is an example of an interstitial

Bioorganometallic chemistry

Bioorganometallic_chemistry

Iron–sulfur protein

Proteins with iron-sulfur clusters

Structure of the FeMoco cluster in nitrogenase. The cluster is linked to the protein by the amino acid residues cysteine and histidine.

Iron–sulfur protein

Iron–sulfur_protein

Metal cluster compound

Cluster of three or more metals

variety of Fe-S clusters have also been identified that have CO as ligands. FeMoco, the active site of most nitrogenases, features a Fe7MoS9C cluster. Zintl

Metal cluster compound