Cytochromes are found in all biological oxidation Systems which involve transport of reducing equivalents through organized chains of membrane bound intermediates, regardless of the ultimate oxidant (Keilin, 1966; Bartsch, 1978; Meyer & Kamen, 1982). Thus, cytochromes are present not only in the aerobic mitochondrial and bac-terial respiratory chain, but are also found in much more diversified procariotic Systems, including all varieties of facultative anaerobes (nitrate and nitrite reducers), obligate anaerobes (sulphate reducers and phototrophic sulphur bacteria), facultative photoheterotrophes (phototrophic non-sulphur purple bacteria), and the photoautotrophic cyanobacteria (blue-green algae). Among the different types of cytochromes occurring in the cell, the soluble c-type cytochromes (‘class I’, Meyer & Kamen, 1982) are the most abundant and best characterized group of proteins (Bartsch, 1978; Meyer & Kamen, 1982; Dickerson & Timkovitch, 1975; Lemberg & Barrett, 1973; Salemme, 1977; Ferguson-Miller, Brautigan & Margoliash, 1979). The amino acid sequences of more than 80 mitochrondrial and close to 40 bacterial cytochromes c are known (Meyer & Kamen, 1982; Dickerson & Timkovitch, 1975; Schwartz & Dayhoff, 1976; Dayhoff & Barker, 1978).

Except when radiation participates, all biological activities involve contact interactions between constituent reactants. At the molecular level, if one of the participants is smaller than its complementary partner, the former is usually designated the ‘ligand’ and the latter the ‘receptor’. Thus in an enzyme–substrate complex, the substrate is the ligand, the enzyme is the receptor. In immunological interactions, the ligand is the hapten or antigen, the receptor is the immunoglobulin. Neurotransmitters or hormones are effector ligands when they are bound to receptor sites at synapses or on cell membranes.

Starting from known properties of non-specific salt effects on the surface tension at an air–water interface, we propose the first general, detailed qualitative molecular mechanism for the origins of ion-specific (Hofmeister) effects on the surface potential difference at an air–water interface; this mechanism suggests a simple model for the behaviour of water at all interfaces (including water–solute interfaces), regardless of whether the non-aqueous component is neutral or charged, polar or non-polar. Specifically, water near an isolated interface is conceptually divided into three layers, each layer being 1 water-molecule thick. We propose that the solute determines the behaviour of the adjacent first interfacial water layer (I1); that the bulk solution determines the behaviour of the third interfacial water layer (I3), and that both I1 and I3 compete for hydrogen-bonding interactions with the intervening water layer (I2), which can be thought of as a transition layer. The model requires that a polar kosmotrope (polar water-structure maker) interact with I1 more strongly than would bulk water in its place; that a chaotrope (water-structure breaker) interact with I1 somewhat less strongly than would bulk water in its place; and that a non-polar kosmotrope (non-polar water-structure maker) interact with I1 much less strongly than would bulk water in its place.

We introduce two simple new postulates to describe the behaviour of I1 water molecules in aqueous solution. The first, the ‘relative competition’ postulate, states that an I1 water molecule, in maximizing its free energy (—δG), will favour those of its highly directional polar (hydrogen-bonding) interactions with its immediate neighbours for which the maximum pairwise enthalpy of interaction (—δH) is greatest; that is, it will favour the strongest interactions. We describe such behaviour as ‘compliant’, since an I1 water molecule will continually adjust its position to maximize these strong interactions. Its behaviour towards its remaining immediate neighbours, with whom it interacts relatively weakly (but still favourably), we describe as ‘recalcitrant’, since it will be unable to adjust its position to maximize simultaneously these interactions. The second, the ‘charge transfer’ postulate, states that the strong polar kosmotrope–water interaction has at least a small amount of covalent character, resulting in significant transfer of charge from polar kosmotropes to water–especially of negative charge from Lewis bases (both neutral and anionic); and that the water-structuring effect of polar kosmotropes is caused not only by the tight binding (partial immobilization) of the immediately adjacent (I1) water molecules, but also by an attempt to distribute among several water molecules the charge transferred from the solute. When extensive, cumulative charge transfer to solvent occurs, as with macromolecular polyphosphates, the solvation layer (the layer of solvent whose behaviour is determined by the solute) can become up to 5- or 6-water-molecules thick.

We then use the ‘relative competition’ postulate, which lends itself to simple diagramming, in conjunction with the ‘charge transfer’ postulate to provide a new, startlingly simple and direct qualitative explanation for the heat of dilution of neutral polar solutes and the temperature dependence of relative viscosity of neutral polar solutes in aqueous solution. This explanation also requires the new and intriguing general conclusion that as the temperature of aqueous solutions is lowered towards o °C, solutes tend to acquire a non-uniform distribution in the solution, becoming increasingly likely to cluster 2 water molecules away from other solutes and surfaces (the driving force for this process being the conversion of transition layer water to bulk water). The implications of these conclusions for understanding the mechanism of action of general (gaseous) anaesthetics and other important interfacial phenomena are then addressed.

The present review describes the methodology of perturbed angular correlation of gamma rays (PAC) applied to biological problems. A large part of the present review focuses on the application of PAC spectroscopy to the study of coordination geometry for the metal site in zinc enzymes. Applications to conformation and dynamics of biomolecules and the use of the method to identify the intracellular sites of either metals or labelled proteins are also discussed.

The non-invasive and non-destructive aspects of NMR and ESR spectroscopy have prompted a variety of research on the pathophysiological impact of murine malaria. NMR is unique in its ability to monitor intracellular pH non-invasively in a heterogeneous sample, a compartmentalized cell and in a whole organism. It has also been shown to be sensitive to unusual structures and metabolic products in free-living protozoa such as Acanthamoeba (Deslauriers et al. 1982a) and Tetrahymena (Deslauriers et al. 1982b; Jarrell et al. 1981). Using the appropriate spin probe, ESR can give valuable information on membrane structure (Schreier, Polnaszek & Smith; 1978). It is particularly useful when quantities of material are limited.

After the work of Marmarelis & Naka (1972, 1973) in the catfish retina, systems analysis using stochastic stimuli has had a boom in the seventies (e.g. McCann & Marmarelis, 1975; Eckert & Bishop, 1975; French & Wong, 1977; Lipson, 1975; McCann, 1974; Naka, Marmarelis & Chan, 1975; Spekreijse & Reits, 1982; Trimble & Phillips, 1978; Terzuolo et al. 1982). White-noise analysis was considered to be a general tool for investigating nonlinear systems gaining a maximum of information with a minimum of assumptions about the system. The modification of the original Wiener theory (Wiener, 1958; Cameron & Martin, 1947; McKean, 1972) by Lee & Schetzen (1965) made the theory fairly easy to implement into widely available computers and thus accessible to a larger number of experimenters.

Theoretical as well as experimental studies of translational accuracy have most often been concerned with the selection of aminoacyl-tRNA by codon-programmed ribosomes. The selection of the successive codons on the mRNA has received much less attention, probably because it represents both conceptually and experimentally, a much more demanding physical problem. Nevertheless, it would seem that errors in the selection of the codon are potentially much more destructive than errors in selection of aminoacyl-tRNA species. This can be appreciated from the following.

Studies of electron-transfer reactions of redox proteins have, in recent years, attracted widespread interest and attention. Progress has been evident from both physical and biological standpoints, with the increasing availability of three-dimensional structural data for many small electron-transfer proteins prompting a variety of systematic investigations (Isied, 1985). Most recently, attention has been directed towards questions concerning the elementary transfer of electrons between spatially remote redox sites, and the nature of protein–protein interactions which, for intermolecular processes, stabilize specific precursor complexes which may be optimally juxtaposed for electron-transfer. These and other issues, including the necessary reversibility of protein interfacial interactions and the dynamic properties of proteins as carriers of electrons in biological electron-transport systems, are now being addressed in the rapidly emerging field of direct (unmediated) protein electrochemistry. It is our intention in this article to discuss developments made in this area and highlight points which we believe to have the most bearing on our current understanding of diffusion-dominated, protein-mediated electron transport at electrode surfaces. First we shall outline some basic considerations which are best considered with reference to homogeneous systems.

Chaos is a widespread and easily recognizable phenomenon that hardly anybody took notice of until recently. The reason may be that chaos has something profoundly counterintuitive about it. It will not fit easily into any familiar cause–effect frame. The best introduction to chaos is by the way of an example. Consider a leaking faucet (Shaw, 1984). When the weight of the accumulating drop exceeds the surface tension the drop falls and a new drop begins to form. If the leak is small and the pressure in the faucet is constant, the time taken for the drop to reach the critical weight is constant. The dripping is perfectly periodic, the period depending on the leak rate. If the leak is slightly increased, the period of dripping will decrease slightly and vice versa. However, somewhere beyond this point the leaking faucet becomes a nuisance. When the leak is increased beyond a certain point the dripping looses its regularity. The time interval between the drops will first alternate periodically between a short and a long time interval. After a further increase of the leak this double periodic pattern will become unstable and change into a new pattern where four different time intervals between the drops alternate periodically. As the leak is further increased the period will double again and again and finally the dripping becomes completely irregular without any repeating pattern. When this occurs we are observing chaos. At the same time we are posed with the problem of understanding how such a ridiculously simple system can show random behaviour.

All living cells require a supply of energy from appropriate metabolic pathways in order in fulfill their physiological functions. A special function common to peripheral nerve fibres and the electroplates of the electric organ is the generation of electrical potentials and a consequent flow of current. A large fraction of their metabolism is therefore devoted basically to maintenance of the unequal distribution of sodium and potassium ions across the cell membranes on which their electrical excitability depends, and involves a consumption of ATP by the membrane-bound Na, K—ATPase system known as the sodium pump.