A model for the mechanism of chloride activation of oxygen evolution in photosystem II.

A hypothesis is proposed to explain the function of Cl(-) in activating the oxygenevolving complex (OEC) of photosystem II (PS II), based on the results of recent (35)Cl-NMR studies. The putative mechanism involves Cl(-) binding to two types of sites. An intrinsic site is suggested to be composed of three histidyl residues (His 332 and His 337 from D1 and His 337 D2).

The rate of formation of P700(+)-A 0 (-) in photosystem I particles from spinach as measured by picosecond transient absorption spectroscopy.

Photosystem I particles containing 30-40 chlorophyll a molecules per primary electron donor P700 were subjected to 1.5 ps low density laser flashes at 610 nm resulting in excitation of the antenna chlorophyll a molecules followed by energy transfer to P700 and subsequent oxidation of P700. Absorbance changes were monitored as a function of time with 1.

Effect of variation of retinal polyene side-chain length on formation and function of bacteriorhodopsin analogue pigments.

The effect of the length of the retinal polyene side chain on bacterioopsin pigment formation and function has been investigated with two series of synthetic retinal analogues. Cyclohexyl derivatives with polyene chains one carbon longer and one or more carbons shorter than retinal and linear polyenes with no ring have been synthesized and characterized. Compounds of six carbons or less in the polyene chain form pigments very poorly or not at all with bacterioopsin.

Mechanism and role of divalent cation binding of bacteriorhodopsin.

Several observations have already suggested that the carboxyl groups are involved in the association of divalent cations with bacteriorhodopsin (Chang et al., 1985). Here we show that at least part of the protons released from deionized purple membrane (;blue membrane') samples when salt is added are from carboxyl groups.

Bicarbonate, not CO2, is the species required for the stimulation of Photosystem II electron transport.

Evidence is presented that the bicarbonate ion (HCO3-), not CO2, H2CO3 or CO32-, is the species that stimulates electron transport in Photosystem II from spinach (Spinacia oleracea). Advantage was taken of the pH dependence of the ratio of HCO3- to CO2 at equilibrium in order to vary effectively the concentration of one species while holding the other constant. The Hill reaction was stimulated in direct proportion with the equilibrium HCO3- concentration, but it was independent of the equilibrium CO2 concentration.

Manganese-histidine cluster as the functional center of the water oxidation complex in photosynthesis.

The recent model of Kambara and Govindjee for water oxidation [Kambara T. and Govindjee (1985) Proc. Natl.

Electron transfer through photosystem II acceptors: Interaction with anions.

We present an overview of anionic interactions with the oxidation-reduction reactions of photosystem II (PSII) acceptors. In section 1, a framework is laid for the electron acceptor side of PSII: the overview begins with a current scheme of the electron transport pathway and of the localization of components in the thylakoid membrane, which is followed by a brief description of the electron acceptor Q or QA and the various heterogeneities associated with it. In section 2, we review briefly the nature of the active species of the bicarbonate (HCO3 (-)) effect, the location of the site of action of HCO3 (-), and its relationship to interactions with other anions.

Molecular mechanism of water oxidation in photosynthesis based on the functioning of manganese in two different environments.

We present a model of photosynthetic water oxidation that utilizes the property of higher-valent Mn ions in two different environments and the characteristic function of redox-active ligands to explain all known aspects of electron transfer from H(2)O to Z, the electron donor to P680, the photosystem II reaction center chlorophyll a. There are two major features of this model. (i) The four functional Mn atoms are divided into two groups of two Mn each: [Mn] complexes in a hydrophobic cavity in the intrinsic 34-kDa protein; and (Mn) complexes on the hydrophilic surface of the extrinsic 33-kDa protein.

Characterization of the chromophore of the third rhodopsin-like pigment of Halobacterium halobium and its photoproduct.

Halobacterium halobium contains at least three retinal-containing pigments: bacteriorhodopsin, halorhodopsin, and a third rhodopsin-like pigment (tR) absorbing at approximately 590 nm, tR590. Illumination of tR590 gives rise to a very long-lived blue absorbing photoproduct, tR370. Using high-performance liquid chromatography we show that the chromophore of tR590 is primarily all-trans retinal and its conversion by light to tR370 causes the chromophore to isomerize primarily to the 13-cis conformation.

Trans/13-cis isomerization is essential for both the photocycle and proton pumping of bacteriorhodopsin.

We studied an analogue of bacteriorhodopsin whose chromophore is based on all-trans retinal. A five-membered ring was built around the 13-14 double bond so as to prohibit trans to 13-cis isomerization. No light-induced photochemical changes were seen, other than those due to a small amount (approximately 5%) of unbleached bacteriorhodopsin remaining in the apomembrane used for regeneration.

The mechanism of photosynthetic water oxidation.

Photosynthetie water oxidation is unique to plants and cyanobacteria, it occurs in thylakoid membranes. The components associated with this process include: a reaction center polypeptide, having a molecular weight (Mr) of 47-50 kilodaltons (kDa), containing a reaction center chlorophyll a labeled as P680, a plastoquinol(?)-electron donor Z, a primary electron acceptor pheophytin, and a quinone electron acceptor QA; three 'extrinsic' polypeptides having Mr of approximately 17 kDa, 23 kDa, and 33 kDa; and, in all likelihood, an approximately 34 kDa 'intrinsic' polypeptide associated with manganese (Mn) atoms. In addition, chloride and calcium ions appear to be essential components for water oxidation.

Cation binding by bacteriorhodopsin.

We have found that extensively washed purple membrane has about 1 calcium and 3-4 magnesium ions bound per bacteriorhodopsin molecule. When these divalent cations are removed by any of a variety of means, the pigment changes its color from purple to blue (lambda(max) approximately 600 nm). This blue pigment, which can be formed at near neutral pH, is probably very similar to blue species formed when the pH of a purple membrane sample is lowered to approximately 2.

A correlation between proton pumping and the bacteriorhodopsin photocycle.

In an attempt to establish a relationship between proton pumping and the photocycle intermediates of bacteriorhodopsin, we have studied the effects of pH and temperature on flash-induced proton pumping and the photointermediates O640 and M412. The relative quantum yield of flash-induced proton pumping is both pH and temperature dependent. It is high in the acid pH range and at low temperatures but decreases in the basic pH range and at high temperatures.

Influence of carbon dioxide concentration during growth on fluorescence induction characteristics of the Green Alga Chlamydomonas reinhardii.

Carbon dioxide concentration during growth is commonly not considered to be a factor influencing the photochemical properties of plants. It was observed that fluorescence induction in Chlamydomonas reinhardii cells grown at air levels of CO2 was both qualitatively and quantitatively different from that of cells grown at 5% CO2. In the two cell types, measured at equivalent chlorophyll and irradiance levels, the fluorescence intensity and the ratio of the levels of peak fluorescence (Fp) to that of the initial fluorescence (Fo) were much lower in the air-adapted than in the 5% CO2 adapted cells.

NMR study of chloride ion interactions with thylakoid membranes.

The role of Cl(-) in photosynthetic O(2) evolution has been investigated by observing the (35)Cl NMR linewidth under a variety of conditions in aqueous suspensions of chloroplasts, primarily for the halophytes Avicennia germinans, Avicennia marina, and Aster tripolium but also for spinach. The line broadening shows there is weak, ionic binding of Cl(-) to thylakoids, the bound Cl(-) exchanging rapidly (>>10(4) sec(-1)) with free Cl(-) in solution. The binding is necessary for O(2) evolution to occur.

Charge accumulation and photochemistry in leaves studied by thermoluminescence and delayed light emission.

A major breakthrough in our understanding of how plants oxidize water to molecular O(2) was the discovery by P. Joliot and co-workers that the O(2) yield per flash, in a series of light flashes, oscillates with a periodicity of 4. This led to the concept by B.

Some plant leaves have orientation-dependent EPR and NMR spectra.

Proton nuclear magnetic resonance ((1)H NMR) spectra of leaves from 50 plant species were obtained at a spectrometer frequency of 470 MHz. Water present in leaf samples gives rise to characteristic spectral patterns. Most species show only one broad (1)H NMR peak; however, the leaves of some plants display complex, orientation-dependent spectra in which a common three-line pattern is discerned.

Effects of pressure and temperature on the M412 intermediate of the bacteriorhodopsin photocycle. Implications for the phase transition of the purple membrane.

The effects of pressure and temperature on the decay kinetics of the M412 (M) intermediate in the photocycle of bacteriorhodopsin were studied to provide information about the phase transitions of the purple membrane lipids. The activation volume (delta V++) for the decay of M is expected to be different below and above a phase transition. However, no abrupt change in delta V++ was found from 3.

Blue light effect on proton pumping by bacteriorhodopsin.

Proton pumping in closed vesicular systems containing bacteriorhodopsin that is initiated by an orange flash, is diminished by a subsequent blue flash. This blue light effect is due to light absorbed by the photocycle intermediate M412 (M), which was formed by the orange flash. A kinetic analysis of the blue-light-induced reduction of proton pumping shows that of the two components of M, only the slowly decaying component is involved in the reduction of proton movement.