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Related Concept Videos

Electron Transport Chain: Complex I and II01:46

Electron Transport Chain: Complex I and II

The mitochondrial electron transport chain (ETC) is the main energy generation system in the eukaryotic cells. However, mitochondria also produce cytotoxic reactive oxygen species (ROS) due to the large electron flow during oxidative phosphorylation. While Complex I is one of the primary sources of superoxide radicals, ROS production by Complex II is uncommon and may only be observed in cancer cells with mutated complexes.
ROS generation is regulated and maintained at moderate levels necessary...
ATP Synthase: Mechanism01:48

ATP Synthase: Mechanism

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 ATP...
ATP Synthase: Structure01:18

ATP Synthase: Structure

ATP synthase or ATPase is among the most conserved proteins found in bacteria, mammals, and plants. This enzyme can catalyze a forward reaction in response to the electrochemical gradient, producing ATP from ADP and inorganic phosphate. ATP synthase can also work in a reverse direction by hydrolyzing ATP and generating an electrochemical gradient. Different forms of ATP synthases have evolved special features to meet the specific demands of the cell. Based on their specific feature, ATP...
Structure of Benzene: Kekulé Model01:07

Structure of Benzene: Kekulé Model

In 1865, August Kekule suggested the structure of benzene according to the structural theory of organic chemistry based on the three assertions—formula of benzene is C6H6, all the hydrogens of benzene are equivalent, and each carbon must have four bonds due to its tetravalency.
He proposed that benzene has a cyclic structure of six carbon atoms attached to one hydrogen atom each, with three alternating pi bonds.
Electrophilic Aromatic Substitution: Sulfonation of Benzene01:22

Electrophilic Aromatic Substitution: Sulfonation of Benzene

Sulfonation of benzene is a reaction wherein benzene is treated with fuming sulfuric acid at room temperature to produce benzenesulfonic acid. Fuming sulfuric acid is a mixture of sulfur trioxide and concentrated sulfuric acid.
Structure of Benzene: Molecular Orbital Model01:18

Structure of Benzene: Molecular Orbital Model

According to the molecular orbital (MO) model, benzene has a planar structure with a regular hexagon of six sp2 hybridized carbons. As shown in Figure 1, each carbon is bonded to three other atoms with C–C–C and H–C–C bond angles of 120°. The C–H bond length is 109 pm, and the C–C bond length is 139 pm which is midway between the single bond length of sp3 hybridized carbons (154 pm) and sp2 hybridized carbons (133 pm).

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Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography
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Published on: September 14, 2014

Subunit structure of benzylsuccinate synthase.

Lei Li1, Dustin P Patterson, Christel C Fox

  • 1Department of Chemistry, University of Michigan, Ann Arbor, Michigan 48109-1055, USA.

Biochemistry
|January 23, 2009
PubMed
Summary

Benzylsuccinate synthase, crucial for anaerobic toluene fermentation, requires coexpression of its gamma-subunit for alpha-subunit expression. The enzyme complex unexpectedly contains iron-sulfur clusters essential for structural integrity.

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Area of Science:

  • Biochemistry
  • Enzymology
  • Microbial Metabolism

Background:

  • Benzylsuccinate synthase (BSS) is a key enzyme in the anaerobic fermentation of toluene.
  • It belongs to the glycyl radical enzyme family and consists of alpha, beta, and gamma subunits.
  • The functions of the beta and gamma subunits were previously unclear.

Purpose of the Study:

  • To investigate the roles of the individual subunits of benzylsuccinate synthase.
  • To characterize the structural and functional properties of the BSS complex.
  • To understand the requirements for efficient expression and assembly of BSS.

Main Methods:

  • Overexpression of BSS subunits (alpha, beta, gamma) in Escherichia coli.
  • Purification of the BSS complex using nickel affinity chromatography.
  • Spectroscopic analysis of iron-sulfur clusters within the BSS complex.

Main Results:

  • Coexpression of the gamma-subunit is necessary for efficient alpha-subunit expression.
  • The purified BSS complex is a hexamer (alpha(2)beta(2)gamma(2)) and contains two [4Fe-4S] iron-sulfur clusters.
  • These iron-sulfur clusters, located on the beta and gamma subunits, are critical for the structural integrity of the enzyme complex.

Conclusions:

  • The gamma-subunit plays a crucial role in stabilizing the alpha-subunit and facilitating BSS complex formation.
  • The identified iron-sulfur clusters are integral components of benzylsuccinate synthase, essential for its structure and likely function.
  • This study elucidates the subunit interactions and structural requirements of benzylsuccinate synthase.