Electron paramagentic resonance studies of photosynthetic electron transport: photoreduction of ferredoxinand membrane-bound iron-sulfur centers.
Electron paramagnetic resonance spectrometry was used to investigate, at physiological temperatures, light-induced electron transport from membrane-bound iron-sulfur components (bound ferredoxin) to soluble ferredoxin and NADP(+) in membrane fragments (from the blue-green alga, Nostoc muscorum) that had high rates of electron transport from water to NADP(+) and from an artificial electron donor, reduced dichlorophenolindophenol (DCIPH(2)) to NADP(+). Illumination at 20 degrees resulted in the photoreduction of membrane-bound iron-sulfur centers A and B. Photoreduction by water gave electron paramagnetic resonance signals of both centers A and B; photoreduction by DCIPH(2) was found to generate a strong electron paramagnetic signal of only center B. When water was the reductant, the addition and photoreduction of soluble ferredoxin generated additional signals characteristics of soluble ferredoxin without causing a decrease in the amplitude of the signals due to centers A and B. The further addition of NADP(+) (and its photoreduction) greatly diminished signals due to the bound iron-sulfur centers and to soluble ferredoxin. An outflow of electrons from center B to soluble ferredoxin and NADP(+) was particularly pronounced when DCIPH(2) was the reductant. These observations provide the first evidence for a light-induced electron transport between membrane-bound iron-sulfur centers and ferredoxin-NADP(+). The relationship of these observations to current concepts of photosynthetic electron transport is discussed.
D000458:Cyanobacteria / Q000378:metabolism; D004578:Electron Spin Resonance Spectroscopy; D004579:Electron Transport; D005288:Ferredoxins / Q000378:metabolism; D007506:Iron-Sulfur Proteins / Q000378:metabolism; D008667:Metalloproteins / Q000378:metabolism; D010084:Oxidation-Reduction; D010788:Photosynthesis
D005288:Ferredoxins; D007506:Iron-Sulfur Proteins; D008667:Metalloproteins