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The cytochrome b6f complex, a member of the cytochrome bc family that mediates energy transduction in photosynthetic and respiratory membranes, is a hetero-oligomeric complex that utilizes two pairs of b-hemes in a symmetric dimer to accomplish trans-membrane electron transfer, quinone oxidation–reduction, and generation of a proton electrochemical potential. Analysis of electron storage in this pathway, utilizing simultaneous measurement of heme reduction, and of circular dichroism (CD) spectra, to assay heme–heme interactions, implies a heterogeneous distribution of the dielectric constants that mediate electrostatic interactions between the four hemes in the complex. Crystallographic information was used to determine the identity of the interacting hemes. The Soret band CD signal is dominated by excitonic interaction between the intramonomer b-hemes, bn and bp, on the electrochemically negative and positive sides of the complex. Kinetic data imply that the most probable pathway for transfer of the two electrons needed for quinone oxidation–reduction utilizes this intramonomer heme pair, contradicting the expectation based on heme redox potentials and thermodynamics, that the two higher potential hemes bn on different monomers would be preferentially reduced. Energetically preferred intramonomer electron storage of electrons on the intramonomer b-hemes is found to require heterogeneity of interheme dielectric constants. Relative to the medium separating the two higher potential hemes bn, a relatively large dielectric constant must exist between the intramonomer b-hemes, allowing a smaller electrostatic repulsion between the reduced hemes. Heterogeneity of dielectric constants is an additional structure–function parameter of membrane protein complexes.

A time-resolved spectroscopic study of the isolated photosynthetic reaction center (RC) from Heliobacterium modesticaldum reveals that thermal equilibration of light excitation among the antenna pigments followed by trapping of excitation and the formation of the charge-separated state P800 (+)A0 (-) occurs within ~25 ps. This time scale is similar to that reported for plant and cyanobacterial photosystem I (PS I) complexes. Subsequent electron transfer from the primary electron acceptor A0 occurs with a lifetime of ~600 ps, suggesting that the RC of H. modesticaldum is functionally similar to that of Heliobacillus mobilis and Heliobacterium chlorum. The (A0 (-) - A0) and (P800 (+) - P800) absorption difference spectra imply that an 8(1)-OH-Chl a F molecule serves as the primary electron acceptor and occupies the position analogous to ec3 (A0) in PS I, while a monomeric BChl g pigment occupies the position analogous to ec2 (accessory Chl). The presence of an intense photobleaching band at 790 nm in the (A0 (-) - A0) spectrum suggests that the excitonic coupling between the monomeric accessory BChl g and the 8(1)-OH-Chl a F in the heliobacterial RC is significantly stronger than the excitonic coupling between the equivalent pigments in PS I.

It is well‐known that treatment of β‐octaethylporphyrin with H2O2/conc. H2SO4 converts it to a β‐oxochlorin as well as all five constitutional isomers of the corresponding β,β’‐dioxo‐derivatives: two bacteriochlorin‐type isomers (β‐oxo groups at opposite pyrrolic building blocks) and three isobacteriochlorin‐type isomers (β‐oxo‐groups at adjacent pyrrolic building blocks). By virtue of the presence of the strongly electronically coupled β‐oxo auxochromes, none of the chromophores are archetypical chlorins, bacteriochlorins, or isobacteriochlorins. Here the authors present, inter alia, the single crystal X‐ray structures of all free‐base diketone isomers and a comparative description of their UV‐vis absorption spectra in neutral and acidic solutions, and fluorescence emission and singlet oxygen photosensitization properties, Magnetic Circular Dichroism (MCD) spectra, and singlet excited state lifetimes. DFT computations uncover underlying tautomeric equilibria and electronic interactions controlling their electronic properties, adding to the understanding of porphyrinoids carrying β‐oxo functionalities. This comparative study lays the basis for their further study and utilization.

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