Bioinorganic chemistry

Source: Wikipedia, the free encyclopedia.
For the journal, see
Bioinorganic Chemistry (journal)
.

Bioinorganic chemistry is a field that examines the role of

non-essential, in medicine and toxicology. Many biological processes such as respiration depend upon molecules that fall within the realm of inorganic chemistry. The discipline also includes the study of inorganic models or mimics that imitate the behaviour of metalloproteins.[1]

As a mix of biochemistry and inorganic chemistry, bioinorganic chemistry is important in elucidating the implications of electron-transfer proteins, substrate bindings and activation, atom and group transfer chemistry as well as metal properties in biological chemistry. The successful development of truly interdisciplinary work is necessary to advance bioinorganic chemistry.[2]

Composition of living organisms

About 99% of

biomolecules in a cell is called the metallome
.

History

Dorothy Crowfoot Hodgkin to consist of a cobalt in a corrin macrocycle. The Watson-Crick structure for DNA
demonstrated the key structural role played by phosphate-containing polymers.

Themes in bioinorganic chemistry

Several distinct systems are of identifiable in bioinorganic chemistry. Major areas include:

Metal ion transport and storage

A diverse collection of

NaKATPase), vacuoles, storage proteins (e.g. ferritin), and small molecules (e.g. siderophores) are employed to control metal ions concentration and bio-availability in living organisms. Crucially, many essential metals are not readily accessible to downstream proteins owing to low solubility in aqueous solutions or scarcity in the cellular environment. Organisms have developed a number of strategies for collecting and transporting such elements while limiting their cytotoxicity
.

Enzymology

Many reactions in life sciences involve water and metal ions are often at the catalytic centers (active sites) for these enzymes, i.e. these are metalloproteins. Often the reacting water is a ligand (see metal aquo complex). Examples of hydrolase enzymes are carbonic anhydrase, metallophosphatases, and metalloproteinases. Bioinorganic chemists seek to understand and replicate the function of these metalloproteins.

Metal-containing electron transfer proteins are also common. They can be organized into three major classes:

copper proteins, and cytochromes. These electron transport proteins are complementary to the non-metal electron transporters nicotinamide adenine dinucleotide (NAD) and flavin adenine dinucleotide (FAD). The nitrogen cycle
make extensive use of metals for the redox interconversions.

4Fe-4S clusters serve as electron-relays in proteins.

Toxicity

Several metal ions are toxic to humans and other animals. The bioinorganic chemistry of lead in the context of its toxicity has been reviewed.[4]

Oxygen transport and activation proteins

Main article: Transition metal dioxygen complex

Aerobic life make extensive use of metals such as iron, copper, and manganese.

oxygen evolving complex present in plants. This system is part of the complex protein machinery that produces oxygen as plants perform photosynthesis
.

Myoglobin is a prominent subject in bioinorganic chemistry, with particular attention to the iron-heme complex that is anchored to the protein.

Bioorganometallic chemistry

organometallic compounds. This area is more focused on the utilization of metals by unicellular organisms. Bioorganometallic compounds are significant in environmental chemistry.[5]

Structure of FeMoco, the catalytic center of nitrogenase.

Metals in medicine

Main article: Metals in medicine

A number of drugs contain metals. This theme relies on the study of the design and mechanism of action of metal-containing pharmaceuticals, and compounds that interact with endogenous metal ions in enzyme active sites. The most widely used anti-cancer drug is

cardiovascular and neuronal importance of nitric oxide has been examined, including the enzyme nitric oxide synthase. (See also: nitrogen assimilation.) Besides, metallic transition complexes based on triazolopyrimidines have been tested against several parasite strains.[6]

Environmental chemistry

Main article: Environmental chemistry

Environmental chemistry traditionally emphasizes the interaction of heavy metals with organisms.

cobalamin
-based enzymes.

Biomineralization

Main article: Biomineralization

Biomineralization is the process by which living organisms produce

vertebrates. Other examples include copper, iron and gold deposits involving bacteria. Biologically-formed minerals often have special uses such as magnetic sensors in magnetotactic bacteria (Fe3O4), gravity sensing devices (CaCO3, CaSO4, BaSO4) and iron storage and mobilization (Fe2O3•H2O in the protein ferritin). Because extracellular[10] iron is strongly involved in inducing calcification,[11][12] its control is essential in developing shells; the protein ferritin plays an important role in controlling the distribution of iron.[13]

Types of inorganic substances in biology

Alkali and alkaline earth metals

Like many antibiotics, monensin-A is an ionophore that tightly bind Na+ (shown in yellow).[14]

The abundant inorganic elements act as

ion channels. For example, muscle contraction depends upon the movement of calcium, sodium and potassium through ion channels in the cell membrane and T-tubules.[17]

Transition metals

The transition metals are usually present as trace elements in organisms, with zinc and iron being most abundant.[18][19][20] These metals are used as protein cofactors and signalling molecules. Many are essential for the activity of enzymes such as catalase and oxygen-carrier proteins such as hemoglobin.[21] These cofactors are tightly to a specific protein; although enzyme cofactors can be modified during catalysis, cofactors always return to their original state after catalysis has taken place. The metal micronutrients are taken up into organisms by specific transporters and bound to storage proteins such as ferritin or metallothionein when not being used.[22][23] Cobalt is essential for the functioning of vitamin B12.[24]

Main group compounds

Many other elements aside from metals are bio-active. Sulfur and phosphorus are required for all life. Phosphorus almost exclusively exists as phosphate and its various esters. Sulfur exists in a variety of oxidation states, ranging from sulfate (SO42−) down to sulfide (S2−). Selenium is a trace element involved in proteins that are antioxidants. Cadmium is important because of its toxicity.[25]

See also

References

  1. ISBN 0-935702-72-5
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    .
  3. ^
    PMID 1872381
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  4. PMID 28731294
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  5. ISBN 978-1-84755-177-1
    .
  6. PMID 29227923
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  7. ISBN 978-0-470-03525-2
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  8. ISBN 978-0-19-504977-0
    .
  9. ISBN 978-0-521-87473-1
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  10. doi:10.1177/11.6.799
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  11. PMID 15295599
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  12. PMID 8312724
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  13. PMID 17845714
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  14. ISBN 978-0-08-037941-8
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  17. PMID 16922804
    .
  18. ISSN 1868-0402
  19. PMID 9498359. Archived from the original
    on 2011-04-30.
  20. PMID 14551660
    .
  21. S2CID 14863354
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  22. PMID 16793761
    .
  23. PMID 17194590
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  24. ISSN 1868-0402
  25. ^ Maret, Wolfgang; Moulis, Jean-Marc (2013). "Chapter 1. The Bioinorganic Chemistry of Cadmium in the Context of its Toxicity". In Astrid Sigel, Helmut Sigel and Roland K. O. Sigel (ed.). Cadmium: From Toxicology to Essentiality. Metal Ions in Life Sciences. Vol. 11. Springer. pp. 1–30.

Literature

External links
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