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R J Cogdell

Publications and source records attributed to R J Cogdell.

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Excited states of photosynthetic reaction centers at low recox potentials.

In preparations of photochemical reaction centers from Rhodopseudomonas spheroides R-26, lowering the recox potential so as to reduce the primary electron acceptor prevents the photochemical transfer of an electron from bacteriochlorophyll to the acceptor. Measuring absorbance changes under these conditions, we found that a 20-ns actinic flash converts the reaction center to a new state, P-F, which then decays with a half-time that is between 1 and 10 ns at 295 degrees K. At 25 degrees K, the decay half-time is approx. 20 ns. The quantum yield of state P-F appears to be near 1.0, both at 295 and at 15 degrees K. State P-F could be an intermediate in the photochemical electron-transfer reaction which occurs when the acceptor is in the oxidized form. Following the decay of state P-F, we detected another state, P-R, with a decay half-time of 6 mus at 295 degrees K and 120 mus at 15 degrees K. The quantum yield of state P-R is approx. 0.1 at 295 degrees K, but rises to a value nearer 1.0 at 15 degrees K. The kinetics and quantum yields are consistent with the view that state P-R forms from P-F. State P-R seems likely to be a side-product, rather than an intermediate in the electron-transfer process. The decay kinetics indicate that state P-F cannot be identical with the lowest excited singlet state of the reaction center. One of the two states, P-F or P-R, probably is the lowest excited triplet state of the reaction center, but it remains unclear which one.

Chlorophyll↗

Picosecond detection of an intermediate in the photochemical reaction of bacterial photosynthesis.

Preparations of photosynthetic reaction centers from Rhodopseudomonas sphaeroides were excited with flashes lasting approximately 8 psec. Immediately after the excitation, there appeared a transient state which was characterized by new absorption bands near 500 and 680 nm, by a bleaching of bands near 540, 600, 760, and 870 nm, and by a blue shift of a band near 800 nm. The transient state decayed with an exponential decay time,t, of 246 plus or minus 16 psec after the flash. As the transient state decayed, the radical cation of the reaction center bacteriochlorophyll complex appeared. This indicates that the transient state is an intermediate in the photooxidation of the bacteriochlorophyll. The absorpiton spectrum of the transient state shows the state to be identical with a state (P-F) which has been detected previously in reaction centers that are prevented from completing the photooxidation, because of chemical reduction of the electron acceptor. Analysis of the spectrum suggests that the formation of P-F involves electron transfer from one bacteriochlorophyll molecule to another within the reaction center, or possibly from bacteriochlorophyll to the bacteriopheophytin of the complex. The initial absorbance changes after flash excitation also include a bleaching of an absorption band at 800 nm. The bleaching decays with tau approximately equal to 30 pse. The bleaching appers not to be a secondary effect, but rather to revael another early step in the primary photochemical reaction.

Bacteriochlorophylls↗

The preparation and characterization of different types of light-harvesting pigment-protein complexes from some purple bacteria.

A general strategy, with some specific examples, is given for the isolation and purification of detergent-soluble, antenna pigment-protein complexes from the photosynthetic membranes. Absorption, fluorescence and circular dichroism spectra, and the pigment and protein composition of B800-B850-protein and B890-protein complexes of some purple bacteria (Rhodospirillum rubrum, Rhodopseudomonas sphaeroides and Rps. capsulata and Chromatium vinosum) are discussed. We conclude that there are probably two major classes of antenna carotenochlorophyll-proteins in purple bacteria containing bacteriochlorophyll a: a B890 complex which has one carotenoid and two bacteriochlorophyll molecules in the minimal unit (probable molecular weight around 20,000), and a B800 + B850 complex which has one carotenoid and three bacteriochlorophyll molecules in a similar-sized minimal unit. The whole cell spectrum of any purple bacterium can be reconstituted by combining different proportions of the spectra of these two complexes with that of the photochemical reaction centre.

Bacterial Proteins↗

The complete amino acid sequences of the B800-850 antenna polypeptides from Rhodopseudomonas acidophila strain 7750.

Spectrally pure B800-850 light harvesting complexes of Rhodopseudomonas acidophila 7750 were prepared by chromatography of LDAO-solubilised photosynthetic membranes on Whatmann DE-52 ion exchange resin. Two low molecular mass polypeptides (alpha, beta) have been isolated by organic solvent extraction of the lyophilised B800-850 light harvesting complexes. Their primary structures were determined by liquid phase sequencer runs, by the sequence analyses of C-terminal o-iodosobenzoic acid fragments, by hydrazinolysis and by carboxypeptidase degradation. B800-850 alpha consists of 53 amino acids and is 45.3% and 50.9% homologous to the B800-850-alpha antenna polypeptides of Rhodobacter sphaeroides and Rhodobacter capsulatus, respectively. The second very short polypeptide (B800-850-beta, 41 amino acids) is 61.0% and 56.1% homologous to the corresponding polypeptides of Rb. sphaeroides and Rb. capsulatus. The molar ratio of the two polypeptides is about 1:1. Both polypeptides show a hydrophilic N-terminal domain, a very hydrophobic central domain and a short C-terminal domain. In both polypeptides the typical His residues, identified in all antenna polypeptides of purple nonsulphur bacteria as possible bacteriochlorophyll binding sites, were found.

Amino Acid Sequence↗