Metalloproteins

Metalloproteins are proteins that bind one or more metal ions or metal-containing cofactors, enabling functions that proteins alone cannot perform. The metal is held in a defined coordination environment by amino acid side chains or other ligands, where it can stabilize structure, transfer electrons, bind oxygen, or activate molecules during catalysis. This chemistry supports essential processes such as respiration, photosynthesis, oxygen transport, and metabolic regulation. Studying metalloproteins helps researchers explain enzyme mechanisms, understand how changes in metal binding affect disease-related pathways, and design biomimetic catalysts, biosensors, and therapeutic strategies.

Metalloproteins - Related Videos

Research

JoVE Journal - Chemistry
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Standards for Quantitative Metalloproteomic Analysis Using Size Exclusion ICP-MS

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Cited by 34 •

2016

Size exclusion chromatography hyphenated with inductively coupled plasma - mass spectrometry (ICP-MS) is a powerful tool to measure changes in the abundance of metalloproteins directly from biological samples. Here we describe a set of metalloprotein standards used to estimate molecular mass and the amount of metal associated with unknown proteins.

Education

JoVE Science Education - Chemistry

Synthesis of an Oxygen-Carrying Cobalt(II) Complex

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2023

Source: Deepika Das, Tamara M. Powers, Department of Chemistry, Texas A&M University Bioinorganic chemistry is the field of study that investigates the role that metals play in biology. Approximately half of all proteins contain metals and it is estimated that up to one third of all proteins rely on metal-containing active sites to function. Proteins that feature metals, called metalloproteins, play a vital role in a variety of cell functions that are necessary for life. Metalloproteins...

Tartrate-Resistant Acid Phosphatase Staining: An In Vitro Technique to Detect TRAP Enzyme-Containing Cultured Osteoclasts

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2025

This video demonstrates the tartrate-resistant acid phosphatase staining technique to detect the presence of TRAP-containing granules inside osteoclasts. The technique forms magenta-colored dye granule deposits in the cytoplasm of osteoclasts, rendering them visible under an inverted microscope.

Research

JoVE Journal - Chemistry
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Monitoring Protein-Ligand Interactions in Human Cells by Real-Time Quantitative In-Cell NMR using a High Cell Density Bioreactor

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Cited by 16 •

2021

This protocol describes the setup of an NMR bioreactor to keep encapsulated human cells viable for up to 72 h, followed by time-resolved in-cell NMR data acquisition and analysis. The methodology is applied to monitor intracellular protein-ligand interactions in real time.

Research

JoVE Journal - Biology
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Detection of Functional Matrix Metalloproteinases by Zymography

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Cited by 126 •

2010

This protocol describes an activity-based assay for detecting matrix metalloproteinases in culture supernatants or body fluids.

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