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Related Concept Videos

Hydrogen Bonds00:26

Hydrogen Bonds

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Hydrogen bonds are weak attractions between atoms that have formed other chemical bonds. One of these atoms is electronegative, like oxygen, and has a partial negative charge. The other is a hydrogen atom that has bonded with another electronegative atom and has a partial positive charge.
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Because hydrogen has very weak electronegativity when it binds with a strongly electronegative atom, such as oxygen or nitrogen, electrons in the bond are unequally shared....
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A hydrogen bond is formed when a weakly positive hydrogen atom already bonded to one electronegative atom (for example, the oxygen in the water molecule) is attracted to another electronegative atom from another polar molecule, such as water (H2O), hydrogen fluoride (HF), or ammonia (NH3). The huge electronegativity difference between the H atom (2.1) and the atom to which it is bonded (4.0 for an F atom, 3.5 for an O atom, or 3.0 for an N atom), combined with the very small size of an H atom...
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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.
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The energy released from the breakdown of the chemical bonds within nutrients can be stored either through the reduction of electron carriers or in the bonds of adenosine triphosphate (ATP). In living systems, a small class of compounds functions as mobile electron carriers, molecules that bind to and shuttle high-energy electrons between compounds in pathways. The principal electron carriers that will be considered originate from the B vitamin group and are derivatives of nucleotides; they are...
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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.
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Related Experiment Video

Updated: Mar 31, 2026

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

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[NiFeSe]-hydrogenase chemistry.

Claire Wombwell1, Christine A Caputo1, Erwin Reisner1

  • 1Christian Doppler Laboratory for Sustainable SynGas Chemistry, Department of Chemistry, University of Cambridge , Lensfield Road, Cambridge CB2 1EW, U.K.

Accounts of Chemical Research
|October 22, 2015
PubMed
Summary
This summary is machine-generated.

[NiFeSe]-hydrogenases are efficient molecular catalysts for renewable hydrogen production via water splitting. These enzymes show high H2 evolution rates, O2 tolerance, and minimal H2 inhibition, making them ideal for artificial photosynthesis.

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Area of Science:

  • Biochemistry and Bioinorganic Chemistry
  • Renewable Energy Technologies
  • Catalysis

Background:

  • Developing inexpensive renewable hydrogen (H2) production via water splitting is crucial for economic, ecological, and humanitarian reasons.
  • Hydrogenases are highly efficient H2 production catalysts, but limitations exist for [FeFe]-hydrogenases (O2 sensitivity) and [NiFe]-hydrogenases (H2 oxidation bias, product inhibition).
  • [NiFeSe]-hydrogenases offer a promising alternative due to their O2 tolerance and high H2 evolution rates with minimal product inhibition.

Purpose of the Study:

  • To explore the unique chemistry and applications of [NiFeSe]-hydrogenases in water splitting technologies.
  • To investigate biomimetic models and semiartificial photosynthetic systems utilizing [NiFeSe]-hydrogenases.
  • To compare the properties of [NiFeSe]-hydrogenases with synthetic models and other hydrogenase classes.

Main Methods:

  • Structural, spectroscopic, and electrochemical analysis of [NiFeSe]-hydrogenases and their synthetic mimics.
  • Development of semiartificial photosynthetic systems integrating [NiFeSe]-hydrogenases with light-harvesting components (e.g., TiO2 nanoparticles, polymeric carbon nitride, organic dyes).
  • Construction of a light-driven full water splitting system using [NiFeSe]-hydrogenase and photosystem II in a photoelectrochemical cell.

Main Results:

  • Synthetic models provided insights into the electronic and reactive effects of selenium in the active site.
  • Enzyme-semiconductor hybrids demonstrated visible light-driven H2 generation with high turnover frequencies (50 s⁻¹).
  • A system with polymeric carbon nitride showed sustained H2 evolution activity for over 2 days, and a full water splitting system was achieved without sacrificial electron donors.

Conclusions:

  • The unique properties of [NiFeSe]-hydrogenases make them highly suitable for efficient and robust molecular H2 evolution.
  • Integration with light-harvesting materials and water oxidation catalysts enables practical artificial photosynthesis for renewable H2 production.
  • [NiFeSe]-hydrogenases represent a key advancement in developing sustainable and scalable water splitting technologies.