Electron and proton transfers from P-430 to ferredoxin-NADP-reductase in Chlorella cells.
After blocking Photosystem II on whole Chlorella cells, we measured the absorption changes between 0 degrees C and -10 degrees C. The absorption changes measured 2 mus after the beginning of a Xenon Flash are the sum of changes due to P(+)-700 and changes due to P(-)-430 (after the subtraction of the carotenoid triplet change and of the electrochromic effect). The reduction of P(-)-430 is not resolved by our technique. Its reoxidation presents a half-time around 1 mus at 0 degrees C and around 2 mus at -10 degrees C. The reduction and protonation of ferredoxin-NADP-reductase to its neutral semi-quinoid form FNRH present a half-time of about 3 mus at 0 degrees C and 6 mus at -10 degrees C. The presence of only one photoreducible ferredoxin-NADP-reductase per Photosystem I center is confirmed, but is an acceptor X' the differential extinction coefficients of which are weak or null from 420 nm to 480 nm. Tentative explanations which would reconcile these results with what was already known about ferredoxin are proposed.
D002708:Chlorella / Q000201:enzymology*; D004579:Electron Transport; D005287:Ferredoxin-NADP Reductase / Q000378:metabolism*; D007506:Iron-Sulfur Proteins / Q000378:metabolism*; D007700:Kinetics; D007834:Lasers; D008667:Metalloproteins / Q000378:metabolism*; D009247:NADH, NADPH Oxidoreductases / Q000378:metabolism*; D010084:Oxidation-Reduction; D010777:Photochemistry; D010788:Photosynthesis; D045331:Photosystem I Protein Complex; D013056:Spectrophotometry, Ultraviolet; D013696:Temperature
D007506:Iron-Sulfur Proteins; D008667:Metalloproteins; D045331:Photosystem I Protein Complex; C024394:P-430; D005287:Ferredoxin-NADP Reductase; D009247:NADH, NADPH Oxidoreductases