Electron transfer reactions biological

The biogeochemical processes that generally describe the interaction of elements with particles are quite well known dissolution, flocculation, ion exchange, sorption, (co)precipitation, electron transfer, and biological uptake. In aquatic environments these reactions often occur simultaneously and competitively. In order to utilize marine tracers effectively, we must understand how elements are associated with particles and sediments. 

The side chains of the 20 different amino acids listed in Panel 1.1 (pp. 6-7) have very different chemical properties and are utilized for a wide variety of biological functions. However, their chemical versatility is not unlimited, and for some functions metal atoms are more suitable and more efficient. Electron-transfer reactions are an important example. Fortunately the side chains of histidine, cysteine, aspartic acid, and glutamic acid are excellent metal ligands, and a fairly large number of proteins have recruited metal atoms as intrinsic parts of their structures among the frequently used metals are iron, zinc, magnesium, and calcium. Several metallo proteins are discussed in detail in later chapters and it suffices here to mention briefly a few examples of iron and zinc proteins. 

The most conspicuous use of iron in biological systems is in our blood, where the erythrocytes are filled with the oxygen-binding protein hemoglobin. The red color of blood is due to the iron atom bound to the heme group in hemoglobin. Similar heme-bound iron atoms are present in a number of proteins involved in electron-transfer reactions, notably cytochromes. A chemically more sophisticated use of iron is found in an enzyme, ribo nucleotide reductase, that catalyzes the conversion of ribonucleotides to deoxyribonucleotides, an important step in the synthesis of the building blocks of DNA. 

Access to three different redox states allows flavin coenzymes to participate in one-electron transfer and two-electron transfer reactions. Partly because of this, flavoproteins catalyze many different reactions in biological systems and work together with many different electron acceptors and donors. These include two-electron acceptor/donors, such as NAD and NADP, one- or two-elec-... 

The field of modified electrodes spans a wide area of novel and promising research. The work dted in this article covers fundamental experimental aspects of electrochemistry such as the rate of electron transfer reactions and charge propagation within threedimensional arrays of redox centers and the distances over which electrons can be transferred in outer sphere redox reactions. Questions of polymer chemistry such as the study of permeability of membranes and the diffusion of ions and neutrals in solvent swollen polymers are accessible by new experimental techniques. There is hope of new solutions of macroscopic as well as microscopic electrochemical phenomena the selective and kinetically facile production of substances at square meters of modified electrodes and the detection of trace levels of substances in wastes or in biological material. Technical applications of electronic devices based on molecular chemistry, even those that mimic biological systems of impulse transmission appear feasible and the construction of organic polymer batteries and color displays is close to industrial use. 

Electron transfer reactions constitute an ubiquitous class of chemical reactions. This is particularly true in biological systems where these reactions often occur at interfaces, in photosynthesis for instance. It is therefore challenging to use the surface specificity and the time resolution of the SHG technique to investigate these processes. At liquid-liquid interfaces, these processes are mimicked through the following scheme ... 

In conclusion therefore it is felt that electrochemistry does offer a valuable technique to study the electron-transfer reactions of biologically-impor-tant molecules. The mechanisms and products observed electrochemically do appear to be similar in many instances to those of the biological reactions. In cases where the biological products or mechanisms are not known electrochemical studies should prove useful in suggesting potential reaction routes and products. 

D.R. McMillin, Purdue University In addition to the charge effects discussed by Professor Sykes, I would like to add that structural effects may help determine electron transfer reactions between biological partners. A case in point is the reaction between cytochrome C551 and azurin where, in order to explain the observed kinetics, reactive and unreactive forms of azurin have been proposed to exist in solution (JL). The two forms differ with respect to the state of protonation of histidine-35 and, it is supposed, with respect to conformation as well. In fact, the lH nmr spectra shown in the Figure provide direct evidence that the nickel(II) derivative of azurin does exist in two different conformations, which interconvert slowly on the nmr time-scale, depending on the state of protonation of the His35 residue (.2) As pointed out by Silvestrini et al., such effects could play a role in coordinating the flow of electrons and protons to the terminal acceptor in vivo. 

If XO is an undoubted historical pioneer among free radical-producing enzymes, whose capacity to catalyze one-electron transfer reactions opened a new era in biological free radical studies, NADPH oxidase is undoubtedly the most important superoxide producer. This enzyme possesses numerous functions from the initiation of phagocytosis to cell signaling, and it is not surprising that its properties have been considered in many reviews during last 20 years [56-58]. 

Electron-transfer reactions at ITIES resemble electron-transfer reactions across biological membranes, which adds a special interest. Also, in contrast to homogeneous electron-transfer reactions, they allow a separation of the reaction products. So it is disappointing to report that only very few experimental investigations of electron-transfer reactions at ITIES have been performed. This is mainly due to the fact that it is difficult to find systems where the reactants do not cross the interface after the reaction in addition, side reactions with the supporting electrolyte can be a problem. 

The NO/NO+ and NO/NO- self-exchange rates are quite slow (42). Therefore, the kinetics of nitric oxide electron transfer reactions are strongly affected by transition metal complexes, particularly by those that are labile and redox active which can serve to promote these reactions. Although iron is the most important metal target for nitric oxide in mammalian biology, other metal centers might also react with NO. For example, both cobalt (in the form of cobalamin) (43,44) and copper (in the form of different types of copper proteins) (45) have been identified as potential NO targets. In addition, a substantial fraction of the bacterial nitrite reductases (which catalyze reduction of NO2 to NO) are copper enzymes (46). The interactions of NO with such metal centers continue to be rich for further exploration. 

A number of electron-transfer reactions of biological interest have been studied using high-pressure techniques (4, 5). These include the oxidation of L-ascorbic acid by [Fe(CN)6]3- (148), [Fe(CN)5N02]3 - (149), and Fe(phen)2(CN)2] (150). The first two reactions are characterized by volumes of activation of -16 and 10 cm3 mol-1, respectively, which indicate that solvent rearrangement as a result of an increase in electrostriction must account for the volume collapse on going to... 

They must be able to undeigo a reasonably fast electron-transfer reaction with the biological redox site... 

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