Heterogeneity of the mechanism of water splitting in photosystem II.
We measured the temperature dependence of oxygen evolution in thylakoids from tobacco using mass spectrometry and high resolution polarography. We determined the initial S-state distribution and the efficiency of the transition between these states including the probability of the O(2) yield through a fast mode. We observed discontinuous changes of the parameters at the temperatures 11 degrees C, 15 degrees C and 21 degrees C. Due to the mass spectroscopy data we think that the irregularity observed at 11 degrees C is due to conformational changes within the water catalytic site. We show that the different contributions of the slow and fast modes of oxygen evolution and of the water molecule exchange are correlated and that their behavior can be explained in terms of the H(2)O accessibility to the water splitting enzyme.
Burda
K
K
Institute of Nuclear Physics, Krakow, Poland.
Schmid
G H
GH
D013058:Mass Spectrometry; D008956:Models, Chemical; D010084:Oxidation-Reduction; D010100:Oxygen / Q000737:chemistry; D010103:Oxygen Isotopes; D010788:Photosynthesis; D045322:Photosynthetic Reaction Center Complex Proteins / Q000737:chemistry*; D045332:Photosystem II Protein Complex; D010947:Plants, Toxic; D011048:Polarography; D013696:Temperature; D020524:Thylakoids / Q000737:chemistry / Q000378:metabolism; D014026:Nicotiana; D014867:Water / Q000737:chemistry*
D010103:Oxygen Isotopes; D045322:Photosynthetic Reaction Center Complex Proteins; D045332:Photosystem II Protein Complex; D014867:Water; D010100:Oxygen