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Electron paramagnetic resonance (EPR) spectroscopy reveals functional and structural similarities between the reaction centres of the chlorophyll d-binding photosystem I (PS I) and chlorophyll a-binding PS I. Continuous wave EPR spectrometry at 12K identifies iron-sulphur centres as terminal electron acceptors of chlorophyll d-binding PS I. A transient light-induced electron spin echo (ESE) signal indicates the presence of a quinone as the secondary electron acceptor (Q) between P(740)(+) and the iron-sulphur centres. The distance between P(740)(+) and Q(-) was estimated within point-dipole approximation as 25.23+/-0.05A, by the analysis of the electron spin echo envelope modulation.

Ammonia and methanol both bind to the water oxidising complex of photosystem II during its turnover, possibly at sites where water binds during the normal water oxidation process. We have investigated the interaction between these two water analogues at the S2 state of the water oxidising cycle using electron magnetic resonance techniques. We find evidence that ammonia displaces methanol from its binding site.

Kinetic analysis using pulsed electron paramagnetic resonance (EPR) of photosynthetic electron transfer in the photosystem I reaction centres of Synechocystis 6803, in wild-type Chlamydomonas reinhardtii, and in site directed mutants of the phylloquinone binding sites in C. reinhardtii, indicates that electron transfer from the reaction centre primary electron donor, P700, to the iron-sulphur centres, Fe-S(X/A/B), can occur through either the PsaA or PsaB side phylloquinone. At low temperature reaction centres are frozen in states which allow electron transfer on one side of the reaction centre only. A fraction always donates electrons to the PsaA side quinone, the remainder to the PsaB side.

The interaction of water oxidising photosystem II preparations with the aqueous environment has been investigated using electron spin echo envelope modulation spectroscopy in the presence of 2H(2)O. The spectra show interaction of 2H of 2H(2)O with the preparation in the S(2) state. The component interacting with water decays during 1-4 weeks storage at 77 K. No interaction of water with the classical multiline S(2) Mn signal, which is more stable on storage at 77 K, was detected. The results show that a component of the water oxidation complex, possibly involving the Mn centre, is accessible to water and may be the water binding site for photosynthetic water oxidation.

Interaction of the water oxidising manganese complex of photosystem II with the aqueous environment has been investigated using electron paramagnetic resonance spectroscopy and electron spin echo envelope modulation spectroscopy to detect interaction of [2H]methanol with the complex in the S2 state. The experiments show that the classical S2 multiline signal is associated with a manganese environment which is not exposed to the aqueous medium. An electron paramagnetic resonance spectroscopy signal, also induced by 200 K illumination, showing 2H modulation by methanol in the medium and a modified multiline electron paramagnetic resonance spectroscopy signal formed in parallel to it, are suggested to be associated with a second manganese environment exposed to the medium.

The radical cation P840+. was studied in frozen suspensions of Chlorobium limicola f. sp. thiosulphatophilum membranes using ENDOR and Special TRIPLE spectroscopies. The spectra show that P840+. arises from a bacteriochlorophyll a 'special' pair with a highly symmetrical distribution of electron spin density between the constituent bacteriochlorophylls. Special TRIPLE spectroscopy has resolved the separate contributions of the two halves of the pair and revealed small deviations from a 1:1 electron spin density distribution. Nevertheless P840+. appears to come the closest yet to the symmetrical 'dimer' originally proposed for the structure of the primary donor radical cation (P870+.) in purple non-sulphur photosynthetic bacteria.

ATP generated by the anaerobic metabolism of L-arginine in Pseudomonas aeruginosa was used to maintain the membrane potential. Although both the ATP concentration and membrane potential were lower than in aerobically incubated bacteria, motility and chemotaxis were almost normal. Venturicidin stopped anaerobic motility by abolishing the membrane potential. The addition of venturicidin to aerobic bacteria caused an increase in the membrane potential, but a decrease in internal ATP concentration, resulting in bacteria which were motile but non-chemotactic. The membrane potential was the only requirement for continued motility but ATP was required in addition for chemotaxis.