The two best-known photophysiological processes are photosynthesis and vision. In photosynthesis light energy is absorbed and transformed into ‘life energy’, in vision the information content of light is utilized by organsims. In photosynthesis chlorophyll and other pigments involved in light-gathering are not chemically changed (except that some of the chlorophyll or phaeophytin molecules are oxidized and immediately reduced again). In human vision the rhodopsin and other visual pigments undergo a reaction cycle induced by photon absorption. The pigment is brought back to its original state only after a long chain of chemical reactions.

In the original Hodgkin & Huxley analysis of the membrane currents in squid giant axon, the time dependence of the currents was attributed to voltage-dependent changes in the permeability of the membrane to the ions involved. According to this theoretical framework, the time constants for the rate of change of current should be unique functions of the membrane potential, and should be independent of the previous history of the voltage and current flowing. In recent years, however, there has been increasing awareness of the fact that, for many physiological preparations, the space just outside the cell membrane is not in good diffusive contact with the bulk extra-cellular fluid perfusing the preparation. Consequently, when current flows across the cell membrane, there are changes in the ion concentrations in this so-called ‘restricted extra-cellular space’ (RECS).

One feature characterizing the transition from prokaryote to eukaryote is the ‘sudden’ appearance of centrioles and their highly structured products, the typical eukaryotic flagella and cilia. These mechanochemical systems appear as fully developed machines, containing some 200 diffierent proteins (Luck et al. 1978) arranged in a remarkably complex organization which has undergone little modification since the advent of the first eukaryotic cells. It is now well established (see, for example, Satir, 1974) that ciliary and flagellar motility is based on a sliding filament mechanism that superficially resembles the far more extensively studied sliding filament system of striated skeletal muscle.The flagellar system, however, appears to be much more complex than the muscle system, because it does not ‘merely’ shorten and generate force, but develops propagating waves and exerts its effects via hydrodynamic interactions with a viscous medium.

Since its introduction, pulse radiolysis has been an important technique for examining the properties of organic and inorganic radicals, and for enumerating those reactions responsible for cellular damage by ionizing radiation. Biochemists, and biophysicists outside the area of radiation biology appear, perhaps for historical reasons, to have an incomplete appreciation of the technique's potential. Protein chemists in particular, have been only dimly aware of the numerous reports of, and the significant results obtained from pulse radiolysis studies of proteins. Our purpose here is to bring some of these results together in order to emphasize the power and usefulness of pulse radiolysis experiments both for elucidating enzyme reaction mechanisms, and for gaining information on the structure of proteins in aqueous solutions. Reviews containing related, or in part the same material to be covered here have appeared previously; for example, Land (1970), Adams et al. (1972a), Shafferman & Stein (1975), Adams & Wardman (1977). This review updates these earlier works, but more importantly approaches the topic of protein pulse radiolysis with a different emphasis.

One of the important problems of biophysics is to understand in detail the mechanisms by which animals produce acoustic signals, and the ways in which other animals, of the same or different species, detect and process these signals, through the masking effects of ambient noise, to extract their information content. At a primitive level this information relates simply to the presence of the other animal and perhaps to its proximity and direction. At the next level we find some sort of coding in the acoustic signal which identifies the species and perhaps the sex, and finally there is the whole range of information content and emotional overtone contained in a complex sound like human speech or music.

Calcium ion plays an essential role in many biological processes. The environment about Ca2+ may be probed by substitution of tripositive lanthanide ions, Ln3+. Ca2+ proteins fall into two broad classes: those that are inhibited by Ln3+ substitution and those that are not. It is suggested that although Ca2+ undertakes a primarily structural role in the Ln3+ non-inhibited proteins, Ca2+ may be near the active site or participate in the mechanism of action of Ln3+ inhibited proteins. Ca2+ and Ln3+ radii are similar; most Ln3+ are slightly larger than Ca2+ in complexes of the same coordination number, and substitution of Ln3+ for Ca2+ is accommodated by a slight decrease in bond distance or by an increase in coordination number. Luminescence from Tb3+ has been demonstrated to be a sensitive environmental probe of Ca2+ binding sites in proteins.

It is generally assumed that the mechanism of enzyme-catalysed reactions would be defined if all the intermediates, complexes and conformational states of each enzyme could be characterized, and the rate-constants for their inter-conversion recorded. In spite of the introduction during the last decades of methods for rapid data acquisition, which permit detection of the number and sequence of intermediates and complexes, measurement of rate-constants, identification of the types of catalysis involved, etc., at best a semi-quantitative understanding of the mechanism of enzyme-catalysis is obtained. The definition of the exact chemical nature of intermediates and complexes is missing because techniques establishing the structures are restricted to the study of transient states which are stable for periods that exceed the half-life of most of typical intermediates. In such conditions, while conformational changes are obviously an essential feature of enzyme activity, the conformational basis of such activity cannot be understood at the molecular level, and enzyme catalysis is still termed a ‘miracle’ compared to the rate-enhancements and specificity of ordinary chemical catalysts.

At the end of the last century it was established that the different nerve cells along a neuronal path do not come into direct physical contact with one another, but that there are narrow gaps between them, called synapses (Sherrington, 1897; Ramón y Cajal, 1906). Elliot (1905) made the basic experimental observation that the propagation of nerve impulses across a synapse might be mediated by specific chemical agents (see Fig. i). Such substances are now called neurotransmitters, and some 20 different compounds putatively responsible for synaptic transmission in different parts of the nervous system are known at present, e.g. a few recently isolated polypeptides. The most extensively studied transmitters are acetylcholine and the catecholamine group, consisting of dopamine (a), noradrenaline (b), and adrenaline (c).

DNA restriction and modification enzymes are responsible for the hostspecific barriers to interstrain and interspecies transfer of genetic information that have been observed in a variety of bacterial cell types. Although the phenomenon of host specificity was initially observed in the early 1950s (Luria & Human, 1952; Bertani & Weigle, 1953), it was nearly a decade later that Arber and his colleagues accurately predicted the molecular basis of the phenomenon. Their experiments with bacteriophage λ demonstrated that a given host-specificity system imparts a specific modification to the viral DNA, and further, that restriction of DNA lacking the appropriate modification is s consquence of nucleolytic hydrolysis upon entry into the host cell (Arber & Dussoix, 1962; Dussoix & Arber, 1962; Arber, Hattman & Dussoix, 1963).

It has virtually become a truism that osmosis, and the inseparable array of related processes comprising ultrafiltration, diffusion, anomalous osmosis, etc., has found its final and lasting exposition to which anything can only be added by way of a few finishing touches. This view, as I shall attempt to show, is quite wrong, if for no other reason than that several of the different approaches to the problem are not complementary. We want two things: to gain an insight into the mechanisms operative in porous systems, and to derive equations which predict the flow rates from a minimal set of properties – if we can decide what these are.

Given the existence of a difference in electrical potential between the interior of a nerve cell and the media surrounding it, where the cytoplasm is some 70 mV negative (Hodgkin, 1958), it must be expected that any positively charged ion to which the cell membrane is permeable is more concentrated in the cell interior. For monovalent cations such as Na and divalent cations such as Ca and Mg this is not the case in the majority of the cells such as the squid giant axon. In other words, nerve cells maintain a lower intracellular concentration of these ions, as compared with their concentration in the extracellular fluid. For Mg, Ca and Na ions, this lower internal concentration must, in the steady state, be effected by some membrane based mechanism which consumes energy.