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Photosystem I

Photosystem I

Although structurally similar to photosystem II (PSII), photosystem I (PSI) is has a different electron supplier and electron acceptor.
Both these photosystems work in concert. An excited electron from PSII is relayed to PSI via an electron transport chain in the thylakoid membrane of the chloroplast, which is comprised of the carrier molecule plastoquinone, the dual-protein cytochrome complex, and plastocyanin. As electrons move between PSII and PSI, they lose energy and must be re-energized...

Microbes and Other Elemental Cycles

Microbes and Other Elemental Cycles

Microbial activity plays a pivotal role in the biogeochemical cycling of iron and manganese, especially at the redox gradients characteristic of stratified aquatic environments. These cycles are driven by microbial transformations between oxidized and reduced forms of the metals, allowing organisms to exploit them for metabolic energy and structural purposes.Iron Cycling Across Redox GradientsIn neutral, oxygen-rich surface waters, iron is predominantly found in its oxidized, insoluble ferric...

Photosystems

Photosystems

Photosystems are multiprotein complexes that form the functional units of photosynthesis in plants, algae, and cyanobacteria. They are found embedded in the membrane of tiny sac-like structures called thylakoids placed inside the chloroplast.
Functioning of Photosystems
Photosystems contain many pigment molecules, such as chlorophylls and carotenoids, arranged in a particular organization across two domains — the antenna complex and the reaction center. The main aim of the pigment molecules...

Anoxygenic Photosynthesis

Anoxygenic Photosynthesis

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 sulfur bacteria, heliobacteria, and...

Electron Transport Chains

Electron Transport Chains

The final stage of cellular respiration is oxidative phosphorylation that consists of two steps: the electron transport chain and chemiosmosis. The electron transport chain is a set of proteins found in the inner mitochondrial membrane in eukaryotic cells. Its primary function is to establish a proton gradient that can be used during chemiosmosis to produce ATP and generate electron carriers, such as NAD+ and FAD, that are used in glycolysis and the citric acid cycle.
The ETC is comprised of...

Sulfur Assimilation

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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Related Experiment Video

Updated: Jun 17, 2026

Laboratory Simulation of an Iron(II)-rich Precambrian Marine Upwelling System to Explore the Growth of Photosynthetic Bacteria

Laboratory Simulation of an Iron(II)-rich Precambrian Marine Upwelling System to Explore the Growth of Photosynthetic Bacteria

Published on: July 24, 2016

Lights on iron-sulfur clusters.

Christopher Horst Lillig¹, Roland Lill

¹Institut für Zytobiologie und Zytopathologie, Philipps-Universität Marburg, Robert-Koch-Strasse 6, 35032 Marburg, Germany.

Chemistry & Biology

|January 13, 2010

Summary

This summary is machine-generated.

Researchers developed a novel, non-invasive fluorescence method to track iron-sulfur cluster formation in cells. This sensitive technique offers a new way to study iron-sulfur protein biogenesis.

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Published on: February 23, 2024

Area of Science:

Biochemistry
Cell Biology
Molecular Biology

Background:

Traditional methods for studying iron-sulfur protein biogenesis, such as enzyme activity assays and radiolabeling, have limitations.
Investigating the complex cellular pathways of iron-sulfur cluster formation is crucial for understanding various biological processes.

Discussion:

Hoff et al. present a groundbreaking, non-invasive fluorescence-based approach for monitoring iron-sulfur cluster formation in living cells.
This new method provides high sensitivity, enabling detailed observation of iron-sulfur protein biogenesis dynamics.

Key Insights:

The fluorescence technique allows for real-time tracking of iron-sulfur cluster assembly within cells.
This advancement overcomes the drawbacks of traditional, often destructive, analytical methods.

Outlook:

This sensitive, non-invasive method is expected to significantly advance the study of iron-sulfur proteins and related cellular mechanisms.
Future research can leverage this technique to explore the roles of iron-sulfur proteins in health and disease.