We have studied van der Waals contacts of the carotenoid rhodopin glucoside (RG) with the bacteriochlorophyll pigments absorbing at 800 nm (B800) in the crystal structure of Rhodopseudomonas acidophila, and the hydrogen positions were determined from quantum chemical calculations at the Hartree--Fock (6-31G) level. We have found strong evidence for hydrogen bonding between the B800 BChl and the RG from neighboring protomer units. The binding energy was estimated to be about 2 kcal/mol (700 cm(-1)). CI-singles approach and time-dependent density functional theory calculations of the B800--RG dimer indicate a red-shift (ca 2 nm) of the B800 Q(y) transition, along with a substantial increase of its oscillator strength, probably due to the hydrogen bonding.
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"It has been reported previously that the puc operon of R. sphaeroides consists of the pucBA (designated puc1BA in the present study) structural genes, whch encode the LHII α-and β-polypeptides, and an additional pucC gene. PucC affects the post-transcriptional expression and assembly of the LHII α-and β-polypeptides[4,5]. In a study of R. sphaeroides mutant construction performed previously, it was observed that following deletion of the puc1BAC genes, there was a second highly homologous "
[Show abstract][Hide abstract] ABSTRACT: The puc2BA operon of Rhodobacter sphaeroides is highly similar to the original puc1BA operon. Genetic, biochemical and spectroscopic approaches were used to investigate the function of puc2BA; the puc1BA and puc2BA structural genes were amplified and cloned into the pRK415 vector controlled by the puc promoter from R. sphaeroides, which was then introduced into R. sphaeroides mutant strains. The results indicated that puc2BA was normally expressed and puc2BA-encoded polypeptides were assembled into membrane LHII (light-harvesting II) complexes, although the puc2A-encoded polypeptide was much larger than the puc1A-encoded polypeptide. Semi-quantitative RT-PCR (reverse transcription-PCR) and SDS/PAGE indicated that puc1BA and puc2BA were expressed in R. sphaeroides when integrated into the genome or expressed from vectors. Furthermore, the polypeptides from the puc1BA and puc2BA genes were both involved in LHII assembly, and pucC is also necessary to assemble LHII complexes. Nevertheless, the LHII complexes synthesized from puc2BA in R. sphaeroides have blue-shift absorption bands at 801 and 846 nm.
[Show abstract][Hide abstract] ABSTRACT: Carotenoids play the dual function of light harvesting and photoprotection in photosynthetic organisms. Despite their functional importance, the molecular basis for binding of carotenoids in the photosynthetic proteins is poorly understood. We have discovered that all carotenoids are surrounded either by aromatic residues or by chlorophylls in all known crystal structures of the photosynthetic pigment-protein complexes. The intermolecular pi-pi stacking interactions between carotenoids and the surrounding aromatic residues in the light-harvesting complex II (LH-II) of Rhodospirillum molischianum were analyzed by high level ab initio electronic structure calculations. Intermolecular interaction energies were calculated with the second-order Møller-Plesset perturbation method (MP2) using the modified 6-31G*(0.25) basis set with diffuse d-polarization by Hobza and co-workers. The MP2/6-31G*(0.25) calculations yield a total stabilization energy of -15.66 kcal/mol between the carotenoid molecule and the four surrounding aromatic residues (alpha-Trp-23, beta-Phe-20, beta-Phe-24, beta-Phe-27). It is thus concluded that pi-pi stacking interactions between carotenoids and the aromatic residues play an essential role in binding carotenoids in the LH-II complex of Rhodospirillum molischianum. The physical nature of the pi-pi stacking interactions was further analyzed, and the dispersion interactions were found to be the dominant intermolecular attraction force. There is also a substantial electrostatic contribution to the overall intermolecular stabilization energy.
Full-text · Article · Aug 2002 · Journal of the American Chemical Society