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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...
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Reaction centers are pigment-protein complexes that initiate energy conversion from photons to chemical entities. Therefore, photochemical reaction center is a more appropriate term that describes these complexes. The Nobel laureates Robert Emerson and William Arnold provided the first experimental evidence of photochemical reaction centers by demonstrating the participation of nearly 2,500 chlorophyll molecules for the release of just one molecule of oxygen. Despite thousands of photosynthetic...
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Anoxygenic photosynthesis is a phototrophic process that captures light energy to drive carbon fixation without producing molecular oxygen. Unlike oxygenic photosynthesis, which utilizes water as an electron donor and releases oxygen, anoxygenic phototrophs use alternative electron donors such as hydrogen sulfide (H₂S), elemental sulfur (S⁰), or thiosulfate (S₂O₃²⁻). This process is carried out by diverse groups of bacteria, including purple bacteria, green...
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    Iron-sulfur clusters are vital ancient cofactors in metabolism and DNA repair. Organisms evolved complex machinery to manage these essential, yet toxic, components, influencing proteome evolution and disease.

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    Area of Science:

    • Biochemistry and Molecular Biology
    • Evolutionary Biology
    • Genomics

    Background:

    • Iron-sulfur clusters are ancient, essential cofactors involved in numerous metabolic processes.
    • Organisms possess specialized machinery (ISC, SUF, CIA) for iron-sulfur cluster synthesis and transfer due to ion toxicity.
    • Iron-sulfur proteins are crucial for fundamental biological functions, including nitrogen fixation, respiration, and DNA processing.

    Purpose of the Study:

    • To analyze the diversity and evolution of iron-sulfur proteomes across different organisms.
    • To understand the relationship between environmental conditions (aerobic/anaerobic) and iron-sulfur cluster composition.
    • To highlight the role of iron-sulfur proteins in cellular compartments and their link to human diseases.

    Main Methods:

    • Genome analysis to predict proteins containing iron-sulfur clusters.
    • Comparative analysis of iron-sulfur proteome size and composition across various organisms.
    • Examination of iron-sulfur protein distribution and function in different cellular compartments.

    Main Results:

    • Iron-sulfur proteomes vary significantly between organisms, correlating with genome size and lifestyle (aerobic vs. anaerobic).
    • Aerobes tend to have smaller proteomes with more [2Fe-2S] clusters, while anaerobes utilize more [4Fe-4S] clusters.
    • Nuclear iron-sulfur proteins play a key role in DNA maintenance in humans.

    Conclusions:

    • The composition of iron-sulfur proteomes reflects evolutionary adaptations to environmental factors like oxygen availability.
    • Dysfunctional iron-sulfur proteins or their biogenesis machinery are linked to severe human diseases.
    • Understanding iron-sulfur cluster biology is critical for comprehending metabolism, evolution, and human health.