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

Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

2.8K
Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...
2.8K
Single-Strand DNA Binding Proteins01:03

Single-Strand DNA Binding Proteins

16.2K
For successful DNA replication, the unwinding of double-stranded DNA must be accompanied by stabilization and protection of the separated single strands of the DNA. This crucial task is performed by single-strand DNA-binding (SSB) proteins. They bind to the DNA in a sequence-independent manner, which means that the nitrogenous bases of the DNA need not be present in a specific order for binding of SSB proteins to it. The binding of SSB proteins straightens single-stranded DNA (ssDNA) and makes...
16.2K
Protein-protein Interfaces02:04

Protein-protein Interfaces

14.3K
Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
14.3K
piRNA - Piwi-interacting RNAs02:57

piRNA - Piwi-interacting RNAs

7.3K
PIWI-interacting RNAs, or piRNAs, are the most abundant short non-coding RNAs. More than 20,000 genes have been found in humans that code for piRNAs while only 2000 genes have been found for miRNAs. piRNAs can act at the transcriptional and post-transcriptional levels and have a vital role in silencing transposable elements present in germ cells. They are also involved in epigenetic silencing and activation. Previously, they were thought to function only in germ cells but new evidence suggests...
7.3K
Cytoskeletal Linker Proteins - Plakins01:09

Cytoskeletal Linker Proteins - Plakins

2.7K
Plakins are large proteins with binding domains for microtubules, microfilaments, intermediate filaments, and membrane-associated protein complexes at cell junctions. Plakin functions are evolutionarily conserved and are primarily involved in organizing the different components of the cytoskeleton by crosslinking them to each other and connecting them to the cell-matrix and cell adhesion complexes. They are also known to interact with signal transducers, serve as scaffolds for signaling...
2.7K
The Replisome03:01

The Replisome

37.5K
DNA replication is carried out by a large complex of proteins that act in a coordinated matter to achieve high-fidelity DNA replication. Together this complex is known as the DNA replication machinery or the replisome.
The synthesis of the leading and lagging strands is a highly coordinated process. To explain this, the “Trombone model” was proposed by Bruce Alberts in 1980. The DNA loop formation starts when a primer is synthesized on the parent lagging strand. The loop grows with...
37.5K

You might also read

Related Articles

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

Sort by
Same author

A structural view of nickel-pincer nucleotide cofactor-related biochemistry.

Critical reviews in biochemistry and molecular biology·2025
Same author

Overcoming barriers for investigating nickel-pincer nucleotide cofactor-related enzymes.

mBio·2024
Same author

Unveiling the mechanisms and biosynthesis of a novel nickel-pincer enzyme.

Biochemical Society transactions·2022
Same author

Validation of an insertion-engineered isoprene synthase as a strategy to functionalize terpene synthases.

RSC advances·2022
Same author

Characterization of the nickel-inserting cyclometallase LarC from Moorella thermoacetica and identification of a cytidinylylated reaction intermediate.

Metallomics : integrated biometal science·2022
Same author

Allelic Variation in the Chloroplast Division Gene <i>FtsZ2-2</i> Leads to Natural Variation in Chloroplast Size.

Plant physiology·2019

Related Experiment Video

Updated: Dec 5, 2025

Split-BioID &#8212; Proteomic Analysis of Context-specific Protein Complexes in Their Native Cellular Environment
09:02

Split-BioID — Proteomic Analysis of Context-specific Protein Complexes in Their Native Cellular Environment

Published on: April 20, 2018

20.2K

Biological pincer complexes.

Jorge Nevarez1, Aiko Turmo2, Jian Hu1,2

  • 1Department of Chemistry, 578 South Shaw Lane, Michigan State University, East Lansing, Michigan 48824 (USA).

Chemcatchem
|October 19, 2020
PubMed
Summary
This summary is machine-generated.

Two biological pincer complexes exist: metal-pyrroloquinolone quinone (PQQ) and nickel-pincer nucleotide (NPN). These cofactors are found in various enzymes across different microorganisms and eukaryotes.

Keywords:
biocatalysisbiosynthesiscofactormetalloenzymenickel

More Related Videos

In Situ Detection of Ribonucleoprotein Complex Assembly in the C. elegans Germline using Proximity Ligation Assay
08:56

In Situ Detection of Ribonucleoprotein Complex Assembly in the C. elegans Germline using Proximity Ligation Assay

Published on: May 5, 2020

6.2K
Dissecting Multi-protein Signaling Complexes by Bimolecular Complementation Affinity Purification BiCAP
06:45

Dissecting Multi-protein Signaling Complexes by Bimolecular Complementation Affinity Purification BiCAP

Published on: June 15, 2018

7.8K

Related Experiment Videos

Last Updated: Dec 5, 2025

Split-BioID &#8212; Proteomic Analysis of Context-specific Protein Complexes in Their Native Cellular Environment
09:02

Split-BioID — Proteomic Analysis of Context-specific Protein Complexes in Their Native Cellular Environment

Published on: April 20, 2018

20.2K
In Situ Detection of Ribonucleoprotein Complex Assembly in the C. elegans Germline using Proximity Ligation Assay
08:56

In Situ Detection of Ribonucleoprotein Complex Assembly in the C. elegans Germline using Proximity Ligation Assay

Published on: May 5, 2020

6.2K
Dissecting Multi-protein Signaling Complexes by Bimolecular Complementation Affinity Purification BiCAP
06:45

Dissecting Multi-protein Signaling Complexes by Bimolecular Complementation Affinity Purification BiCAP

Published on: June 15, 2018

7.8K

Area of Science:

  • Biochemistry
  • Enzymology
  • Bioinorganic Chemistry

Background:

  • Two distinct biological pincer cofactor types are recognized: metal-pyrroloquinolone quinone (PQQ) and nickel-pincer nucleotide (NPN).
  • The PQQ cofactor, an ONO-type complex, is found in bacterial methanol dehydrogenases and other short-chain alcohol dehydrogenases, with metal varying (Ca, Mg, rare earth).
  • The NPN cofactor, an SCS-type complex, is derived from nicotinic acid adenine dinucleotide and identified in lactate racemase (LarA), potentially existing in other bacterial, archaeal, and eukaryotic racemases/epimerases.

Purpose of the Study:

  • To describe the two known types of biological pincer cofactors.
  • To detail the composition and occurrence of PQQ and NPN cofactors.
  • To highlight the enzymatic pathways and organisms associated with these cofactors.

Main Methods:

  • Literature review and comparative analysis of existing biochemical and enzymatic studies.
  • Identification and characterization of PQQ and NPN cofactor structures and biosynthesis pathways.
  • Bioinformatic analysis to predict the distribution of these cofactors in various organisms.

Main Results:

  • The PQQ cofactor is synthesized from a peptide precursor (PqqA) via accessory proteins, forming an ONO-type complex with various metals.
  • The NPN cofactor is biosynthesized from nicotinic acid adenine dinucleotide through specific enzymatic modifications, yielding an SCS-type complex.
  • Both cofactor types are found in diverse microbial and some eukaryotic enzymes, suggesting distinct evolutionary origins and functional roles.

Conclusions:

  • Biological systems utilize at least two distinct pincer cofactor architectures, PQQ and NPN, for enzymatic catalysis.
  • The PQQ and NPN cofactors exhibit unique metal coordination (ONO vs. SCS) and biosynthetic routes.
  • These findings expand our understanding of metalloenzyme diversity and cofactor evolution in prokaryotes and eukaryotes.