Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Nitriles to Carboxylic Acids: Hydrolysis01:08

Nitriles to Carboxylic Acids: Hydrolysis

Nitriles undergo acid-catalyzed hydrolysis or base-catalyzed hydrolysis to form a carboxylic acid. These reactions proceed via an amide intermediate.
Hydrogen Bonds01:04

Hydrogen Bonds

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...
Hydrogen Bonds00:26

Hydrogen Bonds

Hydrogen BondsHydrogen 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.Hydrogen Bonds Control the World!Because hydrogen has very weak electronegativity when it binds with a strongly electronegative atom, such as oxygen or nitrogen, electrons in the bond are...
Electron Transport Chain: Complex I and II01:46

Electron 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...
Reduction of Alkenes: Asymmetric Catalytic Hydrogenation02:17

Reduction of Alkenes: Asymmetric Catalytic Hydrogenation

Catalytic hydrogenation of alkenes is a transition-metal catalyzed reduction of the double bond using molecular hydrogen to give alkanes. The mode of hydrogen addition follows syn stereochemistry.
The metal catalyst used can be either heterogeneous or homogeneous. When hydrogenation of an alkene generates a chiral center, a pair of enantiomeric products is expected to form. However, an enantiomeric excess of one of the products can be facilitated using an enantioselective reaction or an...
Role of Reduced Coenzymes NADH and FADH₂01:29

Role of Reduced Coenzymes NADH and FADH₂

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...

You might also read

Related Articles

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

Sort by
Same author

Quantifying Trace Metals in Gunflint Microfossils by 3D Correlative X-ray Nanoimaging.

Analytical chemistry·2026
Same author

A Structure-Based Analysis of the Evolution of Transcription Factors of the FNR/CRP Family.

Biomolecules·2026
Same author

Stabilisation of the RirA [4Fe-4S] cluster results in loss of iron-sensing function.

Chemical science·2023
Same author

Reflections on the Origin and Early Evolution of the Genetic Code.

Chembiochem : a European journal of chemical biology·2023
Same author

Structural determinants of DNA recognition by the NO sensor NsrR and related Rrf2-type [FeS]-transcription factors.

Communications biology·2022
Same author

Quinolinate Synthase: An Example of the Roles of the Second and Outer Coordination Spheres in Enzyme Catalysis.

Chemical reviews·2022

Related Experiment Video

Updated: Jun 8, 2026

Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase
10:01

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

Published on: December 4, 2017

Structure and Function of [NiFe]-Hydrogenases.

Juan C Fontecilla-Camps1

  • 1Laboratoire de Cristallographie et de Cristallogenèse des Proteines, Institut de Biologie Structurale J. P. Ebel (CEA-CNRS-UJF), 41 rue Jules Horowitz, F-38027 Grenoble Cédex 1, France juan.fontecilla@ibs.fr.

Metal Ions in Life Sciences
|September 30, 2010
PubMed
Summary

Nickel-iron-selenium hydrogenases are microbial enzymes crucial for hydrogen metabolism. Their maturation involves complex machinery, and understanding their oxygen sensitivity is key for biotechnological applications like hydrogen production.

More Related Videos

Expression, Purification, Crystallization, and Enzyme Assays of Fumarylacetoacetate Hydrolase Domain-Containing Proteins
10:21

Expression, Purification, Crystallization, and Enzyme Assays of Fumarylacetoacetate Hydrolase Domain-Containing Proteins

Published on: June 20, 2019

Preparation of SNS Cobalt(II) Pincer Model Complexes of Liver Alcohol Dehydrogenase
06:31

Preparation of SNS Cobalt(II) Pincer Model Complexes of Liver Alcohol Dehydrogenase

Published on: March 19, 2020

Related Experiment Videos

Last Updated: Jun 8, 2026

Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase
10:01

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

Published on: December 4, 2017

Expression, Purification, Crystallization, and Enzyme Assays of Fumarylacetoacetate Hydrolase Domain-Containing Proteins
10:21

Expression, Purification, Crystallization, and Enzyme Assays of Fumarylacetoacetate Hydrolase Domain-Containing Proteins

Published on: June 20, 2019

Preparation of SNS Cobalt(II) Pincer Model Complexes of Liver Alcohol Dehydrogenase
06:31

Preparation of SNS Cobalt(II) Pincer Model Complexes of Liver Alcohol Dehydrogenase

Published on: March 19, 2020

Area of Science:

  • Biochemistry
  • Microbiology
  • Enzymology

Background:

  • [NiFe(Se)]-hydrogenases are hetero-dimeric enzymes catalyzing hydrogen oxidation and proton reduction in microorganisms.
  • These enzymes, like [FeFe]- and [Fe]-hydrogenases, feature a crucial Fe(CO)(x) unit in their active site for hydride binding.
  • Hydrogenases possess complex maturation processes involving nickel and iron transport, cofactor synthesis, and proteolytic cleavage.

Purpose of the Study:

  • To elucidate the intricate maturation machinery of [NiFe(Se)]-hydrogenases.
  • To understand the mechanisms of electron and proton transfer within these enzymes.
  • To investigate the inactivation pathways of [NiFe]-hydrogenases under oxidizing conditions, particularly oxygen exposure.

Main Methods:

  • Analysis of enzyme structure and active site components.
  • Investigation of maturation gene products and their functions.
  • Study of electron transfer pathways mediated by Fe/S clusters.
  • Examination of oxygen inactivation mechanisms and resulting species.

Main Results:

  • The maturation process involves nickel/iron transport, CN(-) and CO synthesis, FeCO(CN(-))(2) unit formation, nickel insertion, and proteolytic cleavage.
  • Electron transfer to the buried active site is facilitated by Fe/S clusters (one or three).
  • Oxygen exposure leads to inactivation, forming oxo or (hydro)peroxo species at the NiFe center, and can modify coordinating thiolates to sulfenates.

Conclusions:

  • [NiFe(Se)]-hydrogenases require extensive maturation machinery for function.
  • Understanding oxygen-induced inactivation mechanisms is vital for their biotechnological application.
  • Further research into these enzymes could advance H(2) production in photosynthetic organisms.