The electron spin relaxation of the electron acceptors of photosystem I reaction centre studied by microwave power saturation
- PMID: 228715
- DOI: 10.1016/0005-2728(79)90064-1
The electron spin relaxation of the electron acceptors of photosystem I reaction centre studied by microwave power saturation
Abstract
Photosystem I particles from spinach were reduced by illumination at 77 K. Under these conditions the one-electrom transfer from P-700 resulted in a reduction of only one acceptor molecule of the reaction centre. The EPR signals at g=2.05, 1.94 and 1.86 were attributed to reduced centre A and the smaller signals at g=2.07, 1.92 and 1.89 to reduced centre B. Reduction of both centres by dithionite in the dark lead to signals at g=2.05, 1.99, 1.96, 1.94, 1.92 and 1.89. Thus, the features at g=2.07 and 1.86 disappeared and new signals at g=1.99 and 1.96 were observed. From the spectral changes it followed that the iron-sulphur centres A and B interact magnetically. Temperature dependent EPR spectra demonstrated a faster electron spin relaxation of centre A than of centre B. These conclusions were corroborated using microwave power saturation of the respective EPR signals. The saturation data of the fully reduced centres A and B could not be fitted using the saturation equation for a one-electron spin system. The magnetic interaction between the (4Fe-4S) CENTRes of the electron acceptors A and B resulted in saturation properties which are simular to those of the 2(4Fe-4S) ferredoxin from Clostridium pasteurianum. For centre X a high proportion of homogeneous broadening of the EPR lines was inferred from the inhomogeneity parameter (b=1.83). It was, therefore, concluded that centre X is most probably an anion radical of chlorophyll. From the low temperature necessary for observing the EPR signal of centre X followed that the drastic relaxation enhancement has to be attributed to a magnetic interaction of the anion radical with iron.
Similar articles
-
Characterization of iron-sulphur centres of plant mitochondria by microwave power saturation.Biochim Biophys Acta. 1979 Oct 10;548(1):16-29. doi: 10.1016/0005-2728(79)90183-x. Biochim Biophys Acta. 1979. PMID: 226132
-
Electron spin relaxation of iron-sulphur proteins studied by microwave power saturation.Biochim Biophys Acta. 1978 Dec 20;537(2):255-60. doi: 10.1016/0005-2795(78)90509-3. Biochim Biophys Acta. 1978. PMID: 215217
-
Comparison of the EPR properties of photosystem I iron-sulphur centres A and B in spinach and barley.Biochim Biophys Acta. 1981 Feb 12;634(2):249-55. doi: 10.1016/0005-2728(81)90143-2. Biochim Biophys Acta. 1981. PMID: 6258648
-
The primary electron acceptor of photosystem. I.Biochim Biophys Acta. 1973 Feb 12;301(1):1-33. doi: 10.1016/0304-4173(73)90010-4. Biochim Biophys Acta. 1973. PMID: 4350387 Review. No abstract available.
-
A survey of EPR investigations of bacterial photosynthesis.Photochem Photobiol. 1976 Dec;24(6):617-28. doi: 10.1111/j.1751-1097.1976.tb06884.x. Photochem Photobiol. 1976. PMID: 190626 Review. No abstract available.
Cited by
-
Crystallization and electron paramagnetic resonance characterization of the complex of photosystem I with its natural electron acceptor ferredoxin.Biophys J. 2002 Oct;83(4):1760-73. doi: 10.1016/S0006-3495(02)73942-8. Biophys J. 2002. PMID: 12324399 Free PMC article.
-
Electron Spin Relaxation and Biochemical Characterization of the Hydrogenase Maturase HydF: Insights into [2Fe-2S] and [4Fe-4S] Cluster Communication and Hydrogenase Activation.Biochemistry. 2017 Jun 27;56(25):3234-3247. doi: 10.1021/acs.biochem.7b00169. Epub 2017 Jun 13. Biochemistry. 2017. PMID: 28525271 Free PMC article.
-
Iron-sulfur centers in the photosynthetic reaction center complex fromChlorobium vibrioforme. Differences from and similarities to the iron-sulfur centers in Photosystem I.Photosynth Res. 1994 Jul;41(1):105-14. doi: 10.1007/BF02184150. Photosynth Res. 1994. PMID: 24310017
-
Reconstitution of iron-sulfur center FB results in complete restoration of NADP (+) photoreduction in Hg-treated Photosystem I complexes from Synechococcus sp. PCC 6301.Photosynth Res. 1995 Nov;46(1-2):249-55. doi: 10.1007/BF00020437. Photosynth Res. 1995. PMID: 24301589
-
Modulation of tension generation at the myofibrillar level -- an analysis of the effect of magnesium adenosine triphosphate, magnesium, pH, sarcomere length and state of phosphorylation.Basic Res Cardiol. 1980 Mar-Apr;75(2):295-317. doi: 10.1007/BF01907579. Basic Res Cardiol. 1980. PMID: 6967310 No abstract available.
MeSH terms
LinkOut - more resources
Full Text Sources