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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...

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Related Experiment Video

Updated: Mar 24, 2026

Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase

Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase

Published on: December 4, 2017

A Functional Model of [Fe]-Hydrogenase.

Tao Xu¹, Chih-Juo Madeline Yin¹, Matthew D Wodrich¹

¹Laboratory of Inorganic Synthesis and Catalysis, Institute of Chemical Sciences and Engineering and ‡Laboratory for Computational Molecular Design, Institute of Chemical Sciences and Engineering, Ecole Polytechnique Fédérale de Lausanne (EPFL) , Lausanne CH-1015, Switzerland.

Journal of the American Chemical Society

|March 2, 2016

Summary

Researchers developed the first iron-based functional mimic of [Fe]-hydrogenase. This novel complex self-activates H2 and catalyzes aldehyde hydrogenation, advancing biomimetic catalysis.

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Last Updated: Mar 24, 2026

Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase

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Published on: March 19, 2020

Area of Science:

Bioinorganic chemistry
Organometallic chemistry
Catalysis

Background:

[Fe]-hydrogenase enzymes catalyze H2 activation and substrate hydrogenation.
Synthetic models of [Fe]-hydrogenase are crucial for understanding enzyme mechanisms.
Existing synthetic models often require external activators for H2 splitting.

Purpose of the Study:

To design and synthesize the first self-activating iron-based functional mimic of the [Fe]-hydrogenase active site.
To investigate the catalytic activity of the model complex in H2 activation and hydrogenation reactions.

Main Methods:

Mechanistic understanding of [Fe]-hydrogenase was employed for rational design.
Synthesis of an iron complex featuring biomimetic pyridinylacyl, carbonyl, and diphosphine ligands with a pendant amine.
Testing the model complex for H2 activation and hydrogenation of an aldehyde substrate.

Main Results:

The synthesized iron complex functions as a self-activating H2-splitting catalyst.
The model complex successfully mediated the hydrogenation of an aldehyde.
The unique ligand environment, including a pendant amine, is key to the complex's activity.

Conclusions:

A novel Fe-based functional mimic of [Fe]-hydrogenase has been achieved.
This model complex demonstrates autonomous H2 activation and catalytic hydrogenation.
The findings provide insights into biomimetic H2 activation and catalysis.