| Genes Encoding A-Type Flavoproteins Are Essential for Photoreduction of O2 in Cyanobacteria Current Biology, Volume 13, Issue 3, 4 February 2003, Pages 230-235 Yael Helman, Dan Tchernov, Leonora Reinhold, Mari Shibata, Teruo Ogawa, Rakefet Schwarz, Itzhak Ohad and Aaron Kaplan Summary O photoreduction by photosynthetic electron transfer, the Mehler reaction , was observed in all groups of oxygenic photosynthetic organisms , but the electron transport chain mediating this reaction remains unidentified. We provide the first evidence for the involvement of A-type flavoproteins that reduce O directly to water in vitro. sp. strain PCC 6803 mutants defective in and , encoding A-type flavoproteins, failed to exhibit O photoreduction but performed normal photosynthesis and respiration. We show that the light-enhanced O uptake was not due to respiration or photorespiration. After dark acclimation, photooxidation of P was severely depressed in mutants Δ and Δ but recovered after light activation of CO fixation, which gives P an additional electron acceptor. Inhibition of CO fixation prevented recovery but scarcely affected P oxidation in the wild-type, where the Mehler reaction provides an alternative route for electrons. We conclude that the source of electrons for O photoreduction is PSI and that the highly conserved A-type flavoproteins Flv1 and Flv3 are essential for this process in vivo. We propose that in cyanobacteria, contrary to eukaryotes, the Mehler reaction produces no reactive oxygen species and may be evolutionarily related to the response of anaerobic bacteria to O. Summary | Full Text | PDF (133 kb) |
| The Photoreduction of Nicotinamide-Adenine Dinucleotide by Chromatophore Fractions from Rhodospirillum rubrum Biophysical Journal, Volume 12, Issue 7, 1 July 1972, Pages 897-908 Rajni Govindjee and Christiaan Sybesma Abstract The photoreduction of nicotinamide-adenine dinucleotide (NAD), catalyzed by chromatophore fractions from young (1 day) and old (4–5 days) cultures of was measured in the presence of either succinate or 2,6-dichlorophenol indophenol (DPIP) and an excess of ascorbate. The time-course of photoreduction in the succinate system suggested a “reversed electron flow” from the donor to NAD mediated by a high energy intermediate produced by a light-induced, cyclic electron transport in the chromatophore fractions. The effects of the uncoupler carbonyl cyanide [-(trifluoromethoxy)phenyl]hydrazone (FCCP) and of the inhibitors antimycin A and 2-heptyl-4-hydroxyquinoline--oxide (HQNO) were consistent with this interpretation. The time-course of NAD photoreduction in the presence of DPIP and ascorbate suggested a direct, light-induced electron transport from the donor to the acceptor. We cannot yet distinguish between a model in which the same reaction center is utilized in the photoreduction by both donor systems (the reaction center component P-870 may relate to two primary acceptors at different redox potential levels) and a model in which each photoreducing system is driven by its own reaction center component. Abstract | PDF (601 kb) |
| Noninvasive Auto-Photoreduction Used as a Tool for Studying Structural Changes in Heme-Copper Oxidases by FTIR Spectroscopy Biophysical Journal, Volume 86, Issue 5, 1 May 2004, Pages 3230-3240 Karin Bettinger, Alexander Prutsch, Karsten Vogtt and Mathias Lübben Abstract We demonstrate an efficient Fourier transform infrared (FTIR) spectroscopic method, termed “auto-photoreduction,” that uses anaerobic photo-induced internal electron transfer to monitor reaction-initiated changes of heme-copper oxidases. It can be applied without the use of either expensive electrochemical equipment, or caged compounds, which cause significant background signals. At high irradiation power, carbon monoxide is released from high-spin heme of cytochrome oxidase and heme from cytochrome . Photochemistry is initiated at wavelengths <355nm, and the photochemical action spectrum has a maximum of 290nm for cytochrome , which is consistent with the possible intermediate involvement of tyrosinate or an activated state of tyrosine. We propose that the final electron donors are proton channel water molecules. In the pH range of 4–9, the noninvasive auto-photoreduction method yields highly reproducible FTIR redox difference spectra within a broad range, resolving a number of vibrational changes outside the amide I region (1600–1640cm). Furthermore, it provides details of redox-induced changes in the spectral region between 1600 and 1100cm. The auto-photoreduction method should be universally applicable to heme proteins. Abstract | Full Text | PDF (214 kb) |
Copyright © 1972 The Biophysical Society. All rights reserved.
Biophysical Journal, Volume 12, Issue 7, 851-857, 1 July 1972
doi:10.1016/S0006-3495(72)86128-9
Article
W.L. Butler
The published reports of flash-induced absorbance changes in the 680–690 nm spectral region, which have been attributed to bleaching of the primary reaction center chlorophyll of photosystem II (PSII) P-680, are discussed in light of what is known about the primary electron acceptor of PSII, C-550. The question of whether the fluorescence yield changes, which accompany the photoreduction of C-550, might influence the measurements of chlorophyll bleaching is examined. The responses attributed to P-680 and their relationship to C-550 indicate that, if the absorbance measurements are valid, P-680 probably functions as the primary electron donor to PSII rather than as a photochemical sensitizer of the primary redox reaction.