Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Redox Reactions

Redox Reactions

Oxidation-reduction or redox reactions involve the transfer of electrons from one molecule or atom to another. When an atom gains an electron, another atom must lose an electron, meaning oxidation and reduction must occur together. Since the redox occurs in pairs, the atom that gets oxidized is also called the reducing agent or reductant, and the atom that is reduced is also called the oxidizing agent or oxidant. A straightforward way to remember the definitions of oxidation and reduction is...

Oxidation Numbers

Oxidation Numbers

In redox reactions, the transfer of electrons occurs between reacting species. Electron transfer is described by a hypothetical number called the oxidation number (or oxidation state). It represents the effective charge of an atom or element, which is assigned using a set of rules.

Formation of Complex Ions

Formation of Complex Ions

A type of Lewis acid-base chemistry involves the formation of a complex ion (or a coordination complex) comprising a central atom, typically a transition metal cation, surrounded by ions or molecules called ligands. These ligands can be neutral molecules like H2O or NH3, or ions such as CN− or OH−. Often, the ligands act as Lewis bases, donating a pair of electrons to the central atom. These types of Lewis acid-base reactions are examples of a broad subdiscipline called coordination...

The Supercomplexes in the Crista Membrane

The Supercomplexes in the Crista Membrane

The mitochondrial cristae membrane is the primary site for the oxidative phosphorylation (OXPHOS) process of energy conversion mediated through respiratory complexes I to V. These complexes have been widely studied for decades, and it has been proven that they form supramolecular structures called respiratory supercomplexes (SC). These higher-order complexes may be crucial in maintaining the biochemical structure and improving the physiological activity of the individual complexes while...

Oxygen Transport in the Blood

Oxygen Transport in the Blood

Hemoglobin (Hb) is a crucial molecule in the human body, consisting of four polypeptide chains, each bound to an iron-containing heme group. This unique structure enables hemoglobin to bind to oxygen, with each molecule capable of combining with four molecules of oxygen, leading to rapid and reversible oxygen loading. When fully loaded with oxygen, it is called oxyhemoglobin, while hemoglobin that has released oxygen is called reduced hemoglobin or deoxyhemoglobin. As hemoglobin binds oxygen,...

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...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

Rational engineering of facultative anaerobiosis enables commensal survival in the oxygenated gut.

bioRxiv : the preprint server for biology·2026

Same author

The physiology and biochemistry of oxidative stress in bacteria.

Advances in microbial physiology·2026

Same author

Fluorescein-based dyes are not valid reporters of oxidative stress in bacteria, and conclusions based on their use must be reconsidered.

Proceedings of the National Academy of Sciences of the United States of America·2025

Same author

The Barrier Properties of Biological Membranes Dictate How Cells Experience Oxidative Stress.

Molecular microbiology·2025

Same author

Evidence for endogenous hydrogen peroxide production by E. coli fatty acyl-CoA dehydrogenase.

PloS one·2024

Same author

Antioxidants are ineffective at quenching reactive oxygen species inside bacteria and should not be used to diagnose oxidative stress.

Molecular microbiology·2024

Search research articles

Related Experiment Video

Updated: Jul 19, 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

Iron-sulphur clusters and the problem with oxygen.

James A Imlay¹

¹Department of Microbiology, University of Illinois, Urbana, IL 61801, USA. jimlay@uiuc.edu

Molecular Microbiology

|January 25, 2006

Summary

Iron-sulfur (Fe-S) clusters were vital for early life, enabling enzymes to transfer electrons and bind metabolites. The rise of oxygen created challenges for Fe-S clusters, impacting microbial evolution and defense mechanisms.

Area of Science:

Biochemistry
Microbial Ecology
Evolutionary Biology

Background:

Early Earth's anaerobic environment fostered the development of iron-sulfur (Fe-S) clusters in proteins.
Fe-S clusters were crucial for ancient enzymes, facilitating electron transfer, metabolite binding, and protein folding.

Purpose of the Study:

To explore the evolutionary impact of Fe-S clusters on life.
To understand how oxygenation affected Fe-S cluster-dependent proteins and microbial strategies.

Main Methods:

Historical analysis of biochemical adaptations.
Review of microbial responses to environmental oxygenation.

Main Results:

Oxygenation led to iron scarcity and Fe-S cluster instability, forcing microbial adaptation.

More Related Videos

Determining the Chemical Composition of Corrosion Inhibitor/Metal Interfaces with XPS: Minimizing Post Immersion Oxidation

Determining the Chemical Composition of Corrosion Inhibitor/Metal Interfaces with XPS: Minimizing Post Immersion Oxidation

Published on: March 15, 2017

Experimental Column Setup for Studying Anaerobic Biogeochemical Interactions Between Iron (Oxy)Hydroxides, Trace Elements, and Bacteria

Experimental Column Setup for Studying Anaerobic Biogeochemical Interactions Between Iron (Oxy)Hydroxides, Trace Elements, and Bacteria

Published on: December 19, 2017

Related Experiment Videos

Last Updated: Jul 19, 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

Determining the Chemical Composition of Corrosion Inhibitor/Metal Interfaces with XPS: Minimizing Post Immersion Oxidation

Determining the Chemical Composition of Corrosion Inhibitor/Metal Interfaces with XPS: Minimizing Post Immersion Oxidation

Published on: March 15, 2017

Experimental Column Setup for Studying Anaerobic Biogeochemical Interactions Between Iron (Oxy)Hydroxides, Trace Elements, and Bacteria

Experimental Column Setup for Studying Anaerobic Biogeochemical Interactions Between Iron (Oxy)Hydroxides, Trace Elements, and Bacteria

Published on: December 19, 2017

Microbes evolved strategies like habitat retreat or antioxidant defenses, with varying success.

Aerobes remain susceptible to iron restriction and oxidative stress due to Fe-S cluster reliance.

Conclusions:

The history of Fe-S clusters profoundly shaped microbial ecology and organismal defense mechanisms.
Fe-S cluster vulnerability continues to influence host-pathogen interactions.