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Properties of Transition Metals

Properties of Transition Metals

Transition metals are defined as those elements that have partially filled d orbitals. As shown in Figure 1, the d-block elements in groups 3–12 are transition elements. The f-block elements, also called inner transition metals (the lanthanides and actinides), also meet this criterion because the d orbital is partially occupied before the f orbitals.

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...

Properties of Organometallic Compounds

Properties of Organometallic Compounds

Organometallic compounds are compounds that contain a carbon–metal bond. Carbon belongs to an organyl group like alkyl, aryl, allyl, or benzyl groups. The metal can be from Group I or Group II of the periodic table, a transition metal, or a semimetal.

Structure and Nomenclature of Thiols and Sulfides

Structure and Nomenclature of Thiols and Sulfides

Thiols and sulfides are sulfur analogs of alcohols and ethers, respectively, where the sulfur atom takes the place of the oxygen atom. Thus, thiols are generally represented as RSH, where R is an alkyl substituent and —SH is the functional group. On the other hand, in sulfides, the central sulfur atom is bonded to two hydrocarbon groups on either side. Depending upon the type of group, sulfides can be either symmetrical or asymmetrical. Both thiols and sulfides display a bent geometry, similar...

Sulfur Assimilation

Sulfur Assimilation

Sulfur is an essential element in biological systems, contributing to synthesizing key biomolecules, including amino acids such as cysteine and methionine, and cofactors such as coenzyme A and biotin. Microorganisms primarily assimilate sulfur as sulfate (SO₄²⁻) from the environment, which must undergo a series of biochemical transformations before it can be incorporated into cellular components. As sulfate is highly oxidized, it must undergo assimilatory sulfate reduction to become...

Bioactivation and Tissue Toxicity

Bioactivation and Tissue Toxicity

Bioactivation is a metabolic process that transforms less reactive substances into highly reactive metabolites, initiating tissue toxicity. This transformation can lead to various toxic effects, including carcinogenesis and teratogenesis. Reactive metabolites are classified into two main types: electrophiles and free radicals.Electrophiles are electron-deficient species and are produced primarily by the enzyme cytochrome P-450 during the metabolism of compounds containing carbon, nitrogen, or...

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Related Experiment Video

Updated: Jul 9, 2026

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

Metallothionein functions and structural characteristics.

Emilio Carpenè¹, Giulia Andreani, Gloria Isani

¹Department of Biochemistry, University of Bologna, Via Tolara di Sopra 50, 40024 Ozzano Emilia, Bologna, Italy. Emilio.Carpene@unibo.it

Journal of Trace Elements in Medicine and Biology : Organ of the Society for Minerals and Trace Elements (GMS)

|December 6, 2007

Summary

This summary is machine-generated.

Metallothioneins (MTs) are cysteine-rich proteins involved in metal binding and antioxidant defense. Their precise functions and roles in diseases linked to metal dysregulation require further investigation.

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Area of Science:

Biochemistry
Molecular Biology
Toxicology

Background:

Metallothioneins (MTs) are small proteins with high cysteine content, forming metal-thiolate clusters.
The mammalian MT gene family includes four subfamilies (MT-1 to MT-4), with specific expression patterns in tissues like brain and epithelial cells.
Despite extensive research on MT structure and function, several aspects remain unclear, including their precise biological roles.

Purpose of the Study:

To review recent literature on metallothioneins.
To highlight MT antioxidant functions and cysteine oxidation.
To explore the link between MTs, metal dysregulation, and disease.

Main Methods:

Literature review of recent experimental data on metallothioneins.
Focus on antioxidant activities and cysteine modifications.
Analysis of MT roles in diseases associated with metal imbalance.

Main Results:

MTs exhibit significant antioxidant functions.
Cysteine oxidation in MTs can lead to intra/intermolecular bridge formation.
MTs are implicated in diseases stemming from metal dysregulation.

Conclusions:

Metallothioneins are crucial in cellular defense mechanisms, particularly against oxidative stress.
Understanding MTs' roles in metal homeostasis and disease pathogenesis is vital.
Further research is needed to fully elucidate the complex functions of these proteins.