Group oxoacids

With concentrated nitric acid, selenium and tellurium form only their +4 oxoacids, H2Se03 and H2Te03 respectively, indicating a tendency for the higher oxidation states to become less stable as the atomic number of the element is increased (cf. Group V, Chapter 9). 

As with the salts of other oxoacids, the thermal stability of nitrates varies markedly with the basicity of the metal, and the products of decomposition are equally varied/ Thus the nitrates of Group 1 and 2 metals find use as molten salt baths because of their thermal stability and low mp (especially as mixtures). Representative values of mp and the temperature (I d) at which the decomposition pressure of O2 reaches 1 atm are ... 

The ricji oxoacid chemistry of sulfur (pp. 705-21) is not paralleled by the heavier elements of the group. The redox relationships have already been summarized (p. 755). Apart from the dark-brown hydrated monoxide Po(OH)2 , which precipitates when alkali is added to a freshly prepared solution of Po(ll), only compounds in the +4 and +6 oxidation states are known. 

The group oxidation state of +5 is too high to allow the formation of simple ionic salts even for Nb and Ta, and in lower oxidation states the higher sublimation energies of these heavier metals, coupled with their ease of oxidation, again militates against the formation of simple salts of the oxoacids. As a consequence the only simple oxoanion salts are the sulfates of vanadium in the oxidation states +3 and +2. These can be crystallized from aqueous solutions as hydrates and are both strongly... 

Halides, 562 Hall, Charles, 3,536 Halogen An element of Group 17,31 oxidizing power of 557 oxoacids of, 567t reactivity, 559 Head-to-head polymer, 613 Head-to-tail polymer, 613 Heat A form of energy that flows between two samples because of their difference in temperature, 197,214 Heat capacity The amount of heat required to raise the temperature one degree Celsius, 199... 

Phosphoric acid, sulfuric acid, and the hydrogen sulfate ion are members of a group of acids known as oxoacids. An oxoacid has a central atom bonded to a variable number of oxygen atoms and OH groups. Except for the three oxoacids shown in Table (sulfuric acid, nitric acid, and perchloric acid), all of the oxoacids described in this textbook are weak acids. Chapter 17 describes in detail the chemistry of strong and weak acids, including carboxylic acids and oxoacids. 

Amino acidi, having donated its amino group becomes an oxoacid (oxoacid2 above) and oxoacidi having accepted the amino group becomes an amino acid (amino acid2). 

As examples, two enzymes that will be discussed again later in this chapter are alanine transaminase (alanine aminotransferase) and aspartate transaminase (aspartate aminotransferase). In both cases, the amino group is transferred to 2-oxoglutarate (also known as a-ketoglutarate), which is oxoacid, above, forming glutamate as amino acid2. For example, the alanine transaminase (ALT) reaction is ... 

Unless the last-mentioned product is removed by the inclusion of catalase, the oxoacid is liable to react further, undergoing oxidative decarboxylation to the carboxylic acid. An attractive feature of this group of enzymes in the present context is that there exist readily available representatives of both enantiospecificities. The well-studied and commercially available AAOs from vertebrate sources, such as l-AAO from snake venom and D-AAO from pig kidney, are expensive, however, and are increasingly being replaced by enzymes from microbial sources. 

A conceptually similar approach applied in an industrial process is described by the Bristol—Myers—Squibb group, who required l-6-OH norleucine as an intermediate in the synthesis of their drug Omapatrilat. T o avoid a lengthy chemical synthesis of the oxoacid, it was more convenient to start with the racemic amino acid, readily prepared by hydrolysis of the corresponding hydantoin (Equation (2)), and remove the D-isomer by oxidation using d-AAO. 

The same group have used the enzyme combination employed in the aspartate deracemization cited above to deracemize 2-naphthylalanine, hut have made use of an interesting innovation introduced by Helaine et al to pull over the poised equilibrium of the transamination reaction. Cysteine sulphinic acid was used as the amino donor in the transamination. The oxoacid product spontaneously decomposes in to pyruvic acid and SO2 (Scheme 3). 

The aminotransferases (ATs) (or transaminases) catalyze the exchange of an amino group between an amino acid and an oxoacid, so that the amino acid is converted into an oxoacid and vice versa (Equation (4)). 

A major aim of amino acid catabolism is removal of the a-NH2 group, which results in the formation of ammonia which is then converted to urea. The removal of the a-NH2 group for most amino acids results in the formation of a carbon-compound, which is usually an oxoacid (e.g. the oxoacid for alanine is pyruvate). 

Transamination is a process in which the oNHa group of an amino acid is removed and the oxoacid is formed. However, the a-NHj group is not lost it is transferred to the oxoacid of another amino acid ... 

For some reactions, the process of transamination is near-equilibrium. This means that amino acids involved can be synthesised from their oxoacid by transfer of the a-NHa group. There are five amino acids in this group ... 

Figure 8.17 The metabolism of branched-chain amino acids in muscle and the fate of the nitrogen and oxoacids. The a-NH2 group is transferred to form glutamate which is then aminated to form glutamine. The ammonia required for aminab on arises from glutamate via glutamate dehydrogenase, but originally from the transamination of the branded chain amino acids. Hence, they provide both nitrogen atoms for glutamine formation.

Thiamine diphosphate (TPP, 3), in cooperation with enzymes, is able to activate aldehydes or ketones as hydroxyalkyl groups and then to pass them on to other molecules. This type of transfer is important in the transketo-lase reaction, for example (see p. 152). Hydroxyalkyl residues also arise in the decarboxylation of 0x0 acids. In this case, they are released as aldehydes or transferred to lipoamide residues of 2-oxoacid dehydrogenases (see p. 134). The functional component of TPP is the sulfur- and nitrogen-containing thiazole ring. 

Pyridoxal phosphate (4) is the most important coenzyme in amino acid metabolism. Its role in transamination reactions is discussed in detail on p. 178. Pyridoxal phosphate is also involved in other reactions involving amino acids, such as decarboxylations and dehydrations. The aldehyde form of pyridoxal phosphate shown here (left) is not generally found in free form. In the absence of substrates, the aldehyde group is covalently bound to the e-amino group of a lysine residue as aldimine ( Schiffs base ). Pyridoxamine phosphate (right) is an intermediate of transamination reactions. It reverts to the aldehyde form by reacting with 2-oxoacids (see p. 178). 

Among the NH2 transfer reactions, transaminations (1) are particularly important. They are catalyzed by transaminases, and occur in both catabolic and anabolic amino acid metabolism. During transamination, the amino group of an amino acid (amino acid 1) is transferred to a 2-oxoacid (oxoacid 2). From the amino acid, this produces a 2-oxo-acid (a), while from the original oxoacid, an amino acid is formed (b). The NH2 group is temporarily taken over by enzyme-bound pyridoxal phosphate (PLP see p. 106), which thus becomes pyridoxamine phosphate. 

Non-essential amino acids are those that arise by transamination from 2-oxoacids in the intermediary metabolism. These belong to the glutamate family (Glu, Gin, Pro, Arg, derived from 2-oxoglutarate), the aspartate family (only Asp and Asn in this group, derived from oxaloacetate), and alanine, which can be formed by transamination from pyruvate. The amino acids in the serine family (Ser, Gly, Cys) and histidine, which arise from intermediates of glycolysis, can also be synthesized by the human body. 

Many of the salts of nitrogenous bases (particularly of high nitrogen content) with oxoacids are imstable or explosive. There are separate group entries for AMINIUM lODATES AND PERIODATES, AMINIUM PERCHLORATES DIAZONIUM PERCHLORATES, DICHROMATE SALTS OE NITROGENOUS BASES I-(I,3-DISELENONYLIDENE)PIPERIDINIUM PERCHLORATES HYDRAZINIUM SALTS, HYDROXYLAMINIUM SALTS... 

Some binary hydrides (e.g. those of Groups 16 and 17) behave as acids in aqueous solution, but the majority of acids are oxoacids derived from acidic oxides. This discussion is restricted to the factors influencing the production of acids or bases when oxides dissolve in water. An oxide can be acidic, amphoteric i.e. acidic or basic depending upon conditions) or basic. 

ANTIMONY-GROUP 6 LIGANDS 28.11.1 Antimony(III) Compounds with Oxoacids... 

Linked oxidation and decarboxylation. Metabolic pathways often make use of oxidation of a (3-hydroxy acid to a (3-oxoacid followed by decarboxylation in the active site of the same enzyme. An example is conversion of L-malate to pyruvate (Eq. 13-45). The Mg2+ or Mn2+-dependent decarboxylating malic dehydrogenase that catalyzes the reaction is usually called the malic enzyme. It is found in most organisms.237-240 While a concerted decarboxylation and dehydrogenation may sometimes occur,241-242 the enzymes of this group appear usually to operate with bound oxoacid intermediates as in Eq. 13-45. 

Chemical studies also support the indicated mechanism. For example, the P-oxoacid intermediate formed in step b of Eq. 13-48 or Fig. 13-12 has been identified as a product released from the enzyme by acid denaturation during steady-state turnover.273 274 Isotopic exchange with 3H in the solvent275 and measurement of 13C isotope effects277 have provided additional verification of the mechanism. The catalytic activity of the enzyme is determined by ionizable groups with pKa values of 7.1 and 8.3 in the ES complex.278... 

Some enzymes contain bound NAD+ which oxidizes a substrate alcohol to facilitate a reaction step and is then regenerated. For example, the malolactic enzyme found in some lactic acid bacteria and also in Ascaris decarboxylates L-malate to lactate (Eq. 15-12). This reaction is similar to those of isocitrate dehydrogenase,110-112 6-phosphogluconate dehydrogenase,113 and the malic enzyme (Eq. 13-45)114 which utilize free NAD+ to first dehydrogenate the substrate to a bound oxoacid whose (3 carbonyl group facilitates decarboxylation. Likewise, the bound NAD+ of the malolactic... 

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