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Compounds of the metallic elements usually form simple aqua ions with the formula [M(H 2 O) n] z+ in low oxidation states. With the higher oxidation states the simple aqua ions dissociate losing hydrogen ions to yield complexes that contain both water molecules and hydroxide or oxide ions, such as the vanadium (IV) species [VO(H 2 O) 5 ] 2+ .
When several metals are linked by metal-metal bonds, the compound or ion is called a metal cluster. Many metal clusters contain several unsupported M–M bonds. Some examples are M 3 (CO) 12 (M = Ru, Os) and Ir 4 (CO) 12. A subclass of unsupported metal–metal bonded arrays are linear chain compounds. In such cases the M–M bonding is weak as ...
The most commonly known and studied bioinorganic iron compounds (biological iron molecules) are the heme proteins: examples are hemoglobin, myoglobin, and cytochrome P450. [1] These compounds participate in transporting gases, building enzymes, and transferring electrons. [5] Metalloproteins are a group of proteins with metal ion cofactors.
The mononuclear Mo enzymes are widely distributed in the biosphere; they catalyze many significant reactions in the metabolism of nitrogen and sulfur-containing compounds as well as various carbonyl compounds (e.g., aldehydes, CO, and CO 2). Nitrate reductases enzymes are important for the nitrogen cycle.
Metal ions and metallic compounds are often used in medical treatments and diagnoses. [18] Compounds containing metal ions can be used as medicine, such as lithium compounds and auranofin. [19] [20] Metal compounds and ions can also produce harmful effects on the body due to the toxicity of several types of metals. [18]
Bioorganometallic chemistry is the study of biologically active molecules that contain carbon directly bonded to metals or metalloids. The importance of main-group and transition-metal centers has long been recognized as important to the function of enzymes and other biomolecules.
The structure of hemoglobin.The heme cofactor, containing the metal iron, shown in green.. Metalloprotein is a generic term for a protein that contains a metal ion cofactor. [1] [2] A large proportion of all proteins are part of this category.
'Nonmolecular' would perhaps be a better term. Metallic bonding is mostly non-polar, because even in alloys there is little difference among the electronegativities of the atoms participating in the bonding interaction (and, in pure elemental metals, none at all). Thus, metallic bonding is an extremely delocalized communal form of covalent bonding.