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Sulfur Assimilation01:20

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Sulfides are the sulfur analog of ethers, just as thiols are the sulfur analog of alcohol. Like ethers, sulfides also consist of two hydrocarbon groups bonded to the central sulfur atom. Depending upon the type of groups present, sulfides can be symmetrical or asymmetrical. Symmetrical sulfides can be prepared via an SN2 reaction between 2 equivalents of an alkyl halide and one equivalent of sodium sulfide.
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Anoxygenic phototrophic bacteria are a diverse group of microorganisms that perform photosynthesis without producing oxygen. They primarily include purple sulfur bacteria, purple nonsulfur bacteria, green sulfur bacteria, and green nonsulfur bacteria. These bacteria are classified into the Gammaproteobacteria, Alphaproteobacteria, Betaproteobacteria, Chlorobi, and Chloroflexi lineages, each with distinct physiological and ecological adaptations.Purple sulfur bacteria belong to the...
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Sulfite-oxidizing enzymes.

Ulrike Kappler1, John H Enemark

  • 1Centre for Metals in Biology, School of Chemistry and Molecular Biosciences, The University of Queensland, St. Lucia, QLD, 4072, Australia, u.kappler@uq.edu.au.

Journal of Biological Inorganic Chemistry : JBIC : a Publication of the Society of Biological Inorganic Chemistry
|September 28, 2014
PubMed
Summary
This summary is machine-generated.

Sulfite-oxidizing enzymes (SOEs) are ancient, essential molybdenum enzymes protecting cells from sulfite damage. Their structure is conserved, but variations in kinetics and electron acceptors exist, with EPR spectroscopy revealing Mo center details.

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Area of Science:

  • Biochemistry
  • Enzymology
  • Bioinorganic Chemistry

Background:

  • Sulfite-oxidizing enzymes (SOEs) are vital molybdenum-containing enzymes found across all life forms.
  • They play a crucial role in cellular protection against sulfite-induced damage.
  • SOEs are evolutionarily ancient, exhibiting conserved domain architecture and fold structure.

Purpose of the Study:

  • To explore the conserved and variable features of sulfite-oxidizing enzymes.
  • To understand the structural and functional diversity within the SOE family.
  • To investigate the role of the molybdenum center and heme groups in SOE catalysis.

Main Methods:

  • Comparative analysis of SOE structures and kinetics.
  • Characterization of molybdenum coordination and cofactor environment.
  • Utilizing Electron Paramagnetic Resonance (EPR) spectroscopy, particularly high-resolution pulsed EPR, to study the Mo center.

Main Results:

  • SOEs share a conserved five-coordinate square pyramidal molybdenum center with a pyranopterin dithiolene cofactor.
  • Significant variations observed in quaternary structure, kinetics, and electron acceptors.
  • Some SOEs possess an integral heme group involved in catalysis.
  • EPR spectroscopy provides insights into the paramagnetic Mo(V) state during turnover.

Conclusions:

  • Sulfite-oxidizing enzymes represent an ancient and diverse enzyme class.
  • Structural and functional plasticity allows adaptation to different cellular environments and electron transfer pathways.
  • EPR spectroscopy is a powerful tool for elucidating the mechanism of molybdenum-based sulfite oxidation.