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Sulfur Assimilation01:20

Sulfur Assimilation

Sulfur is an essential element in biological systems, contributing to synthesizing key biomolecules, including amino acids such as cysteine and methionine, and cofactors such as coenzyme A and biotin. Microorganisms primarily assimilate sulfur as sulfate (SO₄²⁻) from the environment, which must undergo a series of biochemical transformations before it can be incorporated into cellular components. As sulfate is highly oxidized, it must undergo assimilatory sulfate reduction to become...
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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.
Preparation and Reactions of Sulfides02:26

Preparation and Reactions of Sulfides

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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The light reactions of photosynthesis assume a linear flow of electrons from water to NADP+. During this process, light energy drives the splitting of water molecules to produce oxygen. However, oxidation of water molecules is a thermodynamically unfavorable reaction and requires a strong oxidizing agent. This is accomplished by the first product of light reactions: oxidized P680 (or P680+), the most powerful oxidizing agent known in biology. The oxidized P680 that acquires an electron from the...
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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.
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Biosynthesis of the Selenium-Substituted [FeFe]-Hydrogenases.

Xin Yu1, Toby Woods1, Yu Zhang1

  • 1School of Chemical Sciences, University of Illinois, Urbana, Illinois 61801, United States.

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|June 16, 2026
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Researchers replaced sulfur with selenium in the active site of Chlamydomonas reinhardtii [FeFe]-hydrogenase (CrHydA1). This selenium-substituted enzyme (CrHydA1-Se2) exhibits high activity and distinct structural properties compared to the native enzyme.

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Published on: October 18, 2019

Area of Science:

  • Biochemistry
  • Bioinorganic Chemistry
  • Enzyme Engineering

Background:

  • The [FeFe]-hydrogenase enzyme (CrHydA1) from Chlamydomonas reinhardtii is crucial for hydrogen metabolism.
  • Understanding the active site structure-function relationship is key to enzyme engineering and biotechnological applications.
  • Selenium incorporation into metalloenzymes can modulate their catalytic activity and electronic properties.

Purpose of the Study:

  • To prepare a selenium-substituted variant of Chlamydomonas reinhardtii [FeFe]-hydrogenase (CrHydA1-Se2).
  • To investigate the structural, electronic, and catalytic differences between the selenium-substituted and native enzymes.
  • To explore the role of selenium in the active site cofactor maturation process.

Main Methods:

  • HydF-mediated enzyme maturation using a selenium-containing precursor ([HFe2(μ-SeH)(μ-Se)(CN)2(CO)4]2-) and apoenzyme.
  • Structural characterization using 1H and 77Se NMR spectroscopy.
  • Activity assessment and cofactor precursor studies using CH2O.
  • EPR/ENDOR spectroscopy on isotopically pure CrHydA1-77Se2.

Main Results:

  • Efficient production of highly active CrHydA1-Se2 using a selenium-containing precursor and formaldehyde.
  • The selenium-containing precursor ([HFe2(μ-SeH)(μ-Se)(CN)2(CO)4]2-) exhibits a unique hydride structure.
  • Spectroscopic studies confirmed the successful incorporation of selenium and revealed distinct, yet similar, structural and electronic properties of CrHydA1-Se2 compared to native CrHydA1.

Conclusions:

  • Selenium can be successfully incorporated into the active site of CrHydA1, yielding a highly active enzyme variant.
  • The selenium-substituted enzyme possesses unique structural and electronic characteristics influencing its properties.
  • This study provides insights into metalloenzyme maturation and the potential for selenium to modulate hydrogenase function.