Photosynthesis begins with the absorption of light energy and this absorbed energy is transferred to special sites, termed reaction centres. At these sites, the light energy is transformed into chemical products through an oxidation-reduction reaction that generates the primary reactants, an oxidized pigment molecule (P+) and a reduced electron acceptor (A–) (Clayton, 1972). The subsequent reactions of these species in the dark ultimately results in the formation of chemical products required for the fixation of CO2. In this essay we will discuss the nature of the primary reactants generated in the light reactions of chloroplast photosynthesis, stressing recent advances in the identification and characterization of such reactants.

The idea that certain drugs and neurotransmitters produce their effects by combining with specific receptors was first clearly expressed by Langley (1905) on the basis of the selective and localized effect of nicotine on striated muscle fibres. In 1914, Langley published a paper in which the antagonism between ‘curari’ and nicotine was analysed and measured as the ratio by which the nicotine concentration had to be increased in order to produce a standard response in the presence of tubocurarine. It was clear that Langley had in mind the idea of competition between nicotine and curare for the receptor sites and it was surprising that he did not formulatethe theory quantitatively, particularly since Hill, working in Langley's laboratory in 1909, published a mathematical analysis of the action of nicotine on frog muscle giving kinetic and equilibrium equations based on the law of mass action, which could easily have been extended to give an account of competitive antagonism. Barger & Dale (1910) did not favour the idea of specific receptors for sympathomimetic amines.

A distinction has been made between ‘metalloproteins’ and ‘metal-protein complexes’. The former exhibit high metal-ligand stability constants (the metal is not removed during the isolation of the protein), while the latter bind metal ions only loosely (Vallee, 1955). Actually, all proteins can be considered as existing as metal-protein complexes. Selectivity, however, among proteins in their tendency to combine with inorganic ions (both with regard to the type of ion as well as number of ions) suggests that particular configurations produce specific reactive sites. In turn, binding of ions to these sites alters the electronic and consequently the steric conformation of the protein. Thus, effects on macromolecular conformation may not only be due to structural changes of the solvent induced by ions, which modifies solvent-macromole interaction, but also to specific ligation of the ions to the protien which alters local molecular arrangement.

The application of magnetic resonance techniques to biological systems has permitted a detailed study of the nature of the active sites of many proteins that had not been possible previously. Among these is the whole class of iron—sulphur proteins which have been implicated as electron transport proteins in a variety of fundamental processes: photosynthesis, hydroxylation and nitrogen fixation to name but a few.

The single-iron proteins in this class, the rubredoxins, have been studied extensively by chemical, spectroscopic and X-ray crystallographic techniques (Lovenberg, 1973), and the active site is composed of a single iron atom bound in a distorted tetrahedron of cysteine sulphur ligands. The iron is high-spin ferric in the oxidized state and high-spin ferrous in the reduced state. This structure is shown in Fig. I (α).

The current phase of axon physiology began with the invention of the voltage clamp by Cole (1949) and its use by Hodgkin & Huxley (1952d) to produce an astonishingly complete analysis of the ionic permeabilities that are responsible for the action potential. Their description did notcontain much in the way of molecular detail, and left open such questions as whether ions cross the membrane by way of pores or carriers, and the nature of the ‘gating‘ processes that increase ordecrease ion permeability in response to changes of the membrane potential. In the last few years our picture of the ionicchannels has grown considerably more tangible, though it still falls far short of a detailed molecular description. This article describes this sharpened picture and reviews the evidence for it. The viewpoint expressed is a very personal one, andno attempt has been made to review the literature of axonology comprehensively.

It seems to be the membrane bound (Na++K +)-activated enzyme system which transforms the energy from a hydrolysis of ATP into a vectorial movement of sodium out and potassium into the cell against electrochemical gradients, i.e. this systems seems to be the transport system for sodium and potassium (see, for example, review by Skou, 1972; Hokin & Dahl, 1972).

This review is devoted to the presentation of recent developments in a field of theoretical molecular biophysics which seem to open large possibilities for progress in a hitherto relatively unexplored although very important direction. It is concerned with the establishment of a new methodology in the molecular orbital approach to the problem of the solvation of biological molecules. The methodology is still in an initial stage, susceptible of many refinements and its practical applications may also be considered as being in their beginnings. Nevertheless the successes obtained so far and the interest which they aroused in a number of laboratories incite us to present already now the general principles and the available results so as to offer a possibility of evaluating the advantages, present-day limitations and future potentialities of the procedure, which could then be explored by all those interested. This review may thus be said to be to a large extent oriented towards the future, with the acknowledged aim of producing an acceleration and widening of researches in this field. Possible progress in this respect is interesting from a double point of view.

Genetic engineering has quite rightly an image of science fiction. The time when new species with any wanted combination of genetic properties can be ordered from an animal or plant breeding factory seems far away. The layman's view that the science fiction of today is the reality of tomorrow is certainly an insufficient argument to justify optimism. If this were so, we should by now be able to produce hybrids between members of the animal and plant kingdom as was foreseen by a nineteenth-century equivalent of Fred Hoyle (see Fig. I). Despite the scepsis expressed by the prominent scientist Si.r Macfarlane Burnet in his book Genes, Dreams and Realities (1971), recent advances in molecular genetics have raised new enthusiasm (and uneasiness) which make people speak of genetic engineering as something to aim at as an approach to correct inborn errors of metabolism. This will, however, not be our principal dish if we restrict ourselves to a vegetarian menu. We view genetic engineering of plants not only as a future method to improve species, but also as a fundamental approach to the study of gene expression, especially with respect to cell differentiation. If we consider the term literally, the definition of genetic engineering might be any intentional genetic manipulation to alter species or to make new ones. In this sense genetic engineering was practised long before Mendel presented his laws (1865). In the seventeenth century the bulb growers of the Low Countries produced new varieties of tulips for which prices of a thousand forms each were paid (at the 1636 price index!). We notice here already a strong impact of genetic engineering on society; the so-called crazy tulip trade caused a financial disaster on the Amsterdam stock-exchange comparable to the Wall Street crash in the 1930s.

Commercially available electron microscopes routinely provide resolution of some 2–4 Å, as determined on the spacing of crystalline lattices of certain stable, small-molecular substances. On biological material either macromolecules or macromolecular assemblies— ‘biologically significant’ details below some 20 Å have hitherto not been observed.we consider as ‘biologically significant’ those structural details observed or contained in electronmicrographs which are consistent with, or confirmed by, other data obtained from biochemical or functional experiments or by other physical methods (optical, magnetic, electric).

Several reviews have been published recently on the toxicity of heavy metals, but few of these have made any reference to the influence of the nutritional state of animals upon their tolerance of heavy metals. Furthermore, the clinical and metabolic changes occurring as a consequence of increased dietary intake of heavy metals are extremely dependent on factors such as the mineral composition of the diet and nature of the protein source. These aspects will be given particular attention in this review.

A satisfactory understanding of the functions of the sodium pump, the system responsible for the active transport of sodium and potassium, require the isolation and characterization of its protein and lipid components which are integrated in the structure of the cell membrane. The enzyme system (Na+ + K+)-ATPase, is located in membrane fragments and behaves in the test tube like the transport system in the intact cell membrane (Skou,1957) Purified preparations of this enzyme will contain some, if not all, of the components of the sodium pump.