Low-Temperature Interactions of NO with the S1and S2States of the Water-Oxidizing Complex of Photosystem II. A Novel Mn-Multiline EPR Signal Derived from the S1State†

Biochemistry ◽  
1997 ◽  
Vol 36 (30) ◽  
pp. 9261-9266 ◽  
Author(s):  
Charilaos Goussias ◽  
Nikolaos Ioannidis ◽  
Vasili Petrouleas
Keyword(s):  
Low Temperature ◽  
Photosystem Ii ◽  
Epr Signal ◽  
Water Oxidizing Complex ◽  
Temperature Interactions

A Mn(II)−Mn(III) EPR Signal Arises from the Interaction of NO with the S1State of the Water-Oxidizing Complex of Photosystem II†

Biochemistry ◽  
1998 ◽  
Vol 37 (11) ◽  
pp. 3581-3587 ◽  
Author(s):  
Josephine Sarrou ◽  
Nikolaos Ioannidis ◽  
Yannis Deligiannakis ◽  
Vasili Petrouleas
Keyword(s):  
Photosystem Ii ◽  
Epr Signal ◽  
Water Oxidizing Complex

NO Reversibly Reduces the Water-Oxidizing Complex of Photosystem II through S0and S-1to the State Characterized by the Mn(II)-Mn(III) Multiline EPR Signal†

Biochemistry ◽  
1998 ◽  
Vol 37 (47) ◽  
pp. 16445-16451 ◽  
Author(s):  
Nikolaos Ioannidis ◽  
Josephine Sarrou ◽  
Gert Schansker ◽  
Vasili Petrouleas
Keyword(s):  
Photosystem Ii ◽  
The State ◽  
Epr Signal ◽  
Water Oxidizing Complex

Photoactivation of the water-oxidizing complex of photosystem II core complex depleted of functional Mn

1991 ◽  
Vol 1060 (1) ◽  
pp. 51-58 ◽  
Author(s):  
Noriaki Tamura ◽  
Hiroyuki Kamachi ◽  
Nobuyuki Hokari ◽  
Harutoshi Masumoto ◽  
Hiroshi Inoué
Keyword(s):  
Photosystem Ii ◽  
Core Complex ◽  
Water Oxidizing Complex

Site-Directed Mutations of Two Histidine Residues in the D2 Protein Inactivate and Destabilize Photosystem II in the Cyanobacterium Synechocystis 6803

1987 ◽  
Vol 42 (7-8) ◽  
pp. 762-768 ◽  
Author(s):  
Wim F. J. Vermaas ◽  
John G. K. Williams ◽  
Charles J. Arntzen
Keyword(s):  
Low Temperature ◽  
Photosystem Ii ◽  
Purple Bacteria ◽  
Synechocystis 6803 ◽  
Ps Ii ◽  
Histidine Residues ◽  
Fluorescence Maximum ◽  
Herbicide Binding ◽  
Chlorophyll Protein ◽  
D2 Protein

Site-directed mutations were created in the cyanobacterium Synechocystis 6803 to alter specific histidine residues of the photosystem II (PS II) D2 protein. In one mutant (tyr-197). the his-197 residue was replaced by tyrosine, in another mutant (asn-214), his-214 was changed into asparagine. The tyr-197 mutant did not show any low-temperature fluorescence attributable to PS II. but contained a PS II chlorophyll-protein, CP-47, in significant quantities. Another PS II chlorophyll-protein, CP-43, was absent, as was PS II-related herbicide binding. The asn-214 mutant showed a blue-shifted low-temperature fluorescence maximum around 682 nm. but did not have a significant amount of membrane-incorporated CP-43 or CP-47. Herbicide binding was also absent in this mutant. These data indicate a very important role of the his-197 and his-214 residues in the D 2 protein, and are interpreted to support the hypothesis that the D2 protein and the M subunit from the photosynthetic reaction center of purple bacteria have analogous functions. According to this hypothesis, his-197 is involved in binding of P680. and his-214 forms ligands with Qᴀ and Fe2+. In absence of a functional D2 protein, the PS II core complex appears to be destabilized as evidenced by loss of chlorophyll-proteins in the mutants.

The Effects of Low Temperature growth on the Structure of Photosystem II

1984 ◽  
pp. 455-458
Author(s):  
M. Griffith ◽  
M. Krol ◽  
E. L. Camm ◽  
N. P. A. Huner
Keyword(s):  
Low Temperature ◽  
Photosystem Ii ◽  
Temperature Growth ◽  
Low Temperature Growth

scholarly journals Treatment of Cells and Tissues with Chromate Maximizes Mitochondrial 2Fe2S EPR Signals

2019 ◽  
Vol 20 (5) ◽  
pp. 1143 ◽  
Author(s):  
William Antholine ◽  
Jeannette Vasquez-Vivar ◽  
Brendan Quirk ◽  
Harry Whelan ◽  
Pui Wu ◽  
...  
Keyword(s):  
Steady State ◽  
Low Temperature ◽  
Complex I ◽  
White Blood Cells ◽  
Steady State Concentration ◽  
Complex Ii ◽  
Epr Method ◽  
Epr Signal ◽  
State Concentration ◽  
Terminal Cluster

In a previous study on chromate toxicity, an increase in the 2Fe2S electron paramagnetic resonance (EPR) signal from mitochondria was found upon addition of chromate to human bronchial epithelial cells and bovine airway tissue ex vivo. This study was undertaken to show that a chromate-induced increase in the 2Fe2S EPR signal is a general phenomenon that can be used as a low-temperature EPR method to determine the maximum concentration of 2Fe2S centers in mitochondria. First, the low-temperature EPR method to determine the concentration of 2Fe2S clusters in cells and tissues is fully developed for other cells and tissues. The EPR signal for the 2Fe2S clusters N1b in Complex I and/or S1 in Complex II and the 2Fe2S cluster in xanthine oxidoreductase in rat liver tissue do not change in intensity because these clusters are already reduced; however, the EPR signals for N2, the terminal cluster in Complex I, and N4, the cluster preceding the terminal cluster, decrease upon adding chromate. More surprising to us, the EPR signals for N3, the cluster preceding the 2Fe2S cluster in Complex I, also decrease upon adding chromate. Moreover, this method is used to obtain the concentration of the 2Fe2S clusters in white blood cells where the 2Fe2S signal is mostly oxidized before treatment with chromate and becomes reduced and EPR detectable after treatment with chromate. The increase of the g = 1.94 2Fe2S EPR signal upon the addition of chromate can thus be used to obtain the relative steady-state concentration of the 2Fe2S clusters and steady-state concentration of Complex I and/or Complex II in mitochondria.

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