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

Metal-Ligand Bonds

Metal-Ligand Bonds

The hemoglobin in the blood, the chlorophyll in green plants, vitamin B-12, and the catalyst used in the manufacture of polyethylene all contain coordination compounds. Ions of the metals, especially the transition metals, are likely to form complexes.
In these complexes, transition metals form coordinate covalent bonds, a kind of Lewis acid-base interaction in which both of the electrons in the bond are contributed by a donor (Lewis base) to an electron acceptor (Lewis acid). The Lewis acid in...

Cofactors and Coenzymes

Cofactors 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.

Cofactors and Coenzymes

Cofactors 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 and Coenzymes

Cofactors 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.

Microbial Nutrition

Microbial Nutrition

Organisms exhibit remarkable metabolic diversity, categorized based on how they acquire energy and carbon. These strategies enable survival in various ecological niches and are essential for maintaining energy flow and nutrient cycling within ecosystems.Energy and Carbon SourcesOrganisms are classified as phototrophs or chemotrophs based on energy acquisition. Phototrophs use light as their energy source, while chemotrophs rely on oxidizing chemical compounds. Further differentiation arises...

Role of Reduced Coenzymes NADH and FADH₂

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

Multi-lab, multi-enzyme study demonstrates the versatility of bacterial microcompartment shells as a modular platform for confined biocatalysis.

Metabolic engineering·2026

Same author

Quantifying selective metabolite transport for the bacterial microcompartment from <i>Haliangium ochraceum</i> with molecular dynamics simulations.

Nanoscale·2026

Same author

Structures of two LarA-like nickel-pincer nucleotide cofactor-utilizing enzymes with a single catalytic histidine residue.

Protein science : a publication of the Protein Society·2025

Same author

Structures of two LarA-like nickel-pincer nucleotide cofactor-utilizing enzymes with a single catalytic histidine residue.

bioRxiv : the preprint server for biology·2025

Same author

Ancestral Sequence Reconstruction of the Ethylene-Forming Enzyme.

Biochemistry·2025

Same author

Sumner's legacy: a century of urease crystals and recent structural advances.

Critical reviews in biochemistry and molecular biology·2025

Search research articles

Related Experiment Video

Updated: May 7, 2026

Quantification of Metal Leaching in Immobilized Metal Affinity Chromatography

Quantification of Metal Leaching in Immobilized Metal Affinity Chromatography

Published on: January 17, 2020

Nickel-dependent metalloenzymes.

Jodi L Boer¹, Scott B Mulrooney², Robert P Hausinger³

¹Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI 48824, USA.

Archives of Biochemistry and Biophysics

|September 17, 2013

Summary

This summary is machine-generated.

This review details nine nickel-containing enzymes, exploring their diverse structures and catalytic mechanisms. It highlights nickel

Keywords:

Catalytic mechanism Enzyme Metallocenter Nickel Protein structure

More Related Videos

Ion Mobility-Mass Spectrometry Techniques for Determining the Structure and Mechanisms of Metal Ion Recognition and Redox Activity of Metal Binding Oligopeptides

Ion Mobility-Mass Spectrometry Techniques for Determining the Structure and Mechanisms of Metal Ion Recognition and Redox Activity of Metal Binding Oligopeptides

Published on: September 7, 2019

Thermochemical Studies of Ni(II) and Zn(II) Ternary Complexes Using Ion Mobility-Mass Spectrometry

Thermochemical Studies of Ni(II) and Zn(II) Ternary Complexes Using Ion Mobility-Mass Spectrometry

Published on: June 8, 2022

Related Experiment Videos

Last Updated: May 7, 2026

Quantification of Metal Leaching in Immobilized Metal Affinity Chromatography

Quantification of Metal Leaching in Immobilized Metal Affinity Chromatography

Published on: January 17, 2020

Ion Mobility-Mass Spectrometry Techniques for Determining the Structure and Mechanisms of Metal Ion Recognition and Redox Activity of Metal Binding Oligopeptides

Ion Mobility-Mass Spectrometry Techniques for Determining the Structure and Mechanisms of Metal Ion Recognition and Redox Activity of Metal Binding Oligopeptides

Published on: September 7, 2019

Thermochemical Studies of Ni(II) and Zn(II) Ternary Complexes Using Ion Mobility-Mass Spectrometry

Thermochemical Studies of Ni(II) and Zn(II) Ternary Complexes Using Ion Mobility-Mass Spectrometry

Published on: June 8, 2022

Area of Science:

Biochemistry
Enzymology
Bioinorganic Chemistry

Background:

Nickel is a crucial cofactor in various metalloenzymes.
Understanding nickel's role is vital for comprehending diverse biological processes.

Purpose of the Study:

To review the functions, structures, and mechanisms of nine key nickel-containing enzymes.
To explore the diverse metallocenter structures utilized by these enzymes.
To identify other nickel-dependent proteins and their potential roles.

Main Methods:

Literature review of scientific publications.
Analysis of enzyme structures and catalytic mechanisms.
Compilation of known nickel-containing enzymes and proteins.

Main Results:

Detailed descriptions of nine nickel enzymes: glyoxalase I, acireductone dioxygenase, urease, superoxide dismutase, [NiFe]-hydrogenase, carbon monoxide dehydrogenase, acetyl-coenzyme A synthase/decarbonylase, methyl-coenzyme M reductase, and lactate racemase.
Identification of diverse nickel metallocenter structures (mononuclear, dinuclear, Ni-Fe, clusters, tetrapyrroles).
Note on other nickel-active enzymes with unclear physiological relevance and unidentified nickel proteins.

Conclusions:

Nickel plays a significant role in a wide array of enzyme functions.
The diversity in nickel metallocenter structures reflects the varied catalytic activities.
Further research is needed to elucidate the physiological relevance of some nickel-enzyme interactions and the functions of uncharacterized nickel proteins.