Heat-stress stimulation of electron flow in a photosystem I submembrane fraction.
Oxygen uptake using methyl viologen as the terminal electron acceptor was recorded in digitonin-derived photosystem I submembrane fractions incubated at either 25 or 50 degrees C. A two- to four-fold heat-stress stimulation of electron flow was detected at 50 degrees C when reduced 2,6-dichlorophenol-indophenol was used as the primary electron donor. However, no stimulation was seen with N,N,N',N'-tetramethylphenylenediamine as the donor. The stimulation was enhanced by specific cations (Mg2+, Na+, K+), but not by Mn2 or Ca2+. The enhancement obtained with Mg2+ could be eliminated by incubating for a prolonged period. It is proposed that the observed heat-stress stimulation is due to a conformational change at the level of the cytochrome b6-f complex. This change increased the affinity of the protein complex for 2,6-dichlorophenol-indophenol at its oxidation sites. The involvement of a conformational modification is demonstrated by the absence of heat-stress stimulation in submembrane fractions immobilized in an albumin-glutaraldehyde cross-linked matrix.
Boucher
N
N
Centre de recherche en photobiophysique, Université du Québec à Trois-Rivières, Canada.
Harnois
J
J
Carpentier
R
R
D015086:2,6-Dichloroindophenol / Q000378:metabolism; D002462:Cell Membrane / Q000378:metabolism; D003573:Cytochrome b Group / Q000378:metabolism; D045346:Cytochrome b6f Complex; D004072:Digitonin; D004583:Electrons; D006358:Hot Temperature; D007425:Intracellular Membranes / Q000378:metabolism; D007700:Kinetics; D010084:Oxidation-Reduction; D010100:Oxygen / Q000378:metabolism; D045322:Photosynthetic Reaction Center Complex Proteins / Q000378:metabolism*; D045331:Photosystem I Protein Complex
D003573:Cytochrome b Group; D045322:Photosynthetic Reaction Center Complex Proteins; D045331:Photosystem I Protein Complex; D045346:Cytochrome b6f Complex; D015086:2,6-Dichloroindophenol; D004072:Digitonin; D010100:Oxygen