Related Experiment Video
Updated: May 12, 2026
![Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase](/_next/image?url=https%3A%2F%2Fcloudfront.jove.com%2FCDNSource%2Fteasers%2F55858.jpg&w=3840&q=50)
10:01
Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase
Published on: December 4, 2017
[Fe]-hydrogenase and models that contain iron-acyl ligation
Katherine M Schultz1, Dafa Chen, Xile Hu
1Laboratory of Inorganic Synthesis and Catalysis, Institute of Chemical Sciences and Engineering, Ecole Polytechnique Fédérale de Lausanne (EPFL), SB-ISIC-LSCI, BCH 3305, Lausanne, CH 1015, Switzerland.
Chemistry, an Asian Journal
|April 19, 2013
Summary
Newly discovered [Fe]-hydrogenase enzymes split hydrogen using a unique iron-acyl active site. Synthetic iron-acyl complexes mimic this enzyme, advancing our understanding of hydrogenase mechanisms.
Area of Science:
- Biochemistry
- Bioinorganic Chemistry
- Enzyme Catalysis
Background:
- [Fe]-hydrogenase is a recently identified enzyme class.
- It catalyzes heterolytic hydrogen splitting with natural substrates.
- The active site features a unique mono-iron center with iron-acyl ligation.
Purpose of the Study:
- To review studies on [Fe]-hydrogenase.
- To discuss synthetic iron-acyl complexes as enzyme models.
- To highlight recent research in this field.
Main Methods:
- Literature review of [Fe]-hydrogenase research.
- Analysis of synthetic iron-acyl complex studies.
- Focus on in-house experimental findings.
Main Results:
- [Fe]-hydrogenase utilizes a distinct active site for hydrogen activation.
- Synthetic models replicate key structural and functional aspects of the enzyme.
- Ongoing research provides insights into the catalytic mechanism.
Conclusions:
- [Fe]-hydrogenase represents a significant advancement in hydrogenase research.
- Synthetic models are crucial for elucidating the enzyme's mechanism.
- Further investigation promises deeper understanding of bio-inspired catalysis.
Related Concept Videos
01:43Electron Transport Chain: Complex III and IV
During the electron transport chain, electrons from NADH and FADH2 are first transferred to complexes I and II, respectively. These two complexes then transfer the electrons to ubiquinol, which carries them further to complex III. Complex III passes the electrons across the intermembrane space to Cyt c, which carries them further to complex IV. Complex IV donates electrons to oxygen and reduces it to water. As electrons pass through complexes I, III, and IV, the energy released aids the pumping...
01:46Electron Transport Chain: Complex I and II
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.
ROS generation is regulated and maintained at moderate levels necessary...
ROS generation is regulated and maintained at moderate levels necessary...
01:28Electron 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...
The ETC is comprised of...
01:29Electron Transport Chain Components
The electron transport chain (ETC) is a crucial metabolic pathway that facilitates energy conversion in prokaryotic and eukaryotic cells. In eukaryotes, the ETC comprises four membrane-associated protein complexes in the inner mitochondrial membrane. In prokaryotes, the ETC in the plasma membrane can vary in composition, with fewer or different complexes depending on the organism and environmental conditions. These complexes transfer electrons from electron donors, such as NADH and FADH2, to...
01:24Cofactors and Coenzymes
Enzymes are proteins made of amino acids. The functional group of each constituent amino acid catalyzes a wide variety of chemical reactions via ionic interactions or acid-base reactions. However, amino acids cannot catalyze oxidation-reduction and group transfer reactions and need to be aided by non-protein components called cofactors. Cofactors are also referred to as the chemical teeth of an enzyme.
Cofactors can be metallic ions or organic molecules called coenzymes. These types of helper...
Cofactors can be metallic ions or organic molecules called coenzymes. These types of helper...
01:27Cofactors and Coenzymes
Enzymes require additional components for proper function. There are two such classes of molecules: cofactors and coenzymes. Cofactors are metallic ions and coenzymes are non-protein organic molecules. Both of these types of helper molecule can be tightly bound to the enzyme or bound only when the substrate binds.