Changes in Structural and Functional Properties of Oxygen-evolving Complex Induced by Replacement of D1-Glutamate 189 with Glutamine in Photosystem II

@article{Kimura2005ChangesIS,
  title={Changes in Structural and Functional Properties of Oxygen-evolving Complex Induced by Replacement of D1-Glutamate 189 with Glutamine in Photosystem II},
  author={Y. Kimura and N. Mizusawa and A. Ishii and S. Nakazawa and T. Ono},
  journal={Journal of Biological Chemistry},
  year={2005},
  volume={280},
  pages={37895 - 37900}
}
A carboxylate group of D1-Glu-189 in photosystem II has been proposed to serve as a direct ligand for the manganese cluster. Here we constructed a mutant that eliminates the carboxylate by replacing D1-Glu-189 with Gln in the cyanobacterium Synechocystis sp. PCC 6803, and we examined the resulting effects on the structural and functional properties of the oxygen-evolving complex (OEC) in photosystem II. The E189Q mutant grew photoautotrophically, and isolated photosystem II core particles… Expand
Participation of glutamate-354 of the CP43 polypeptide in the ligation of manganese and the binding of substrate water in photosystem II.
In the current X-ray crystallographic structural models of photosystem II, Glu354 of the CP43 polypeptide is the only amino acid ligand of the oxygen-evolving Mn(4)Ca cluster that is not provided byExpand
Substitution of the D1-Asn87 site in photosystem II of cyanobacteria mimics the chloride-binding characteristics of spinach photosystem II
TLDR
Steady-state O2-evolution activity assays revealed that substitution of the D1 residue at position 87 with alanine perturbs the chloride-binding site in the proton-exit channel and provide new insight into the role ofThe D1-Asn87 site inThe water-oxidation mechanism and explain the difference in the chloridebinding properties of cyanobacterial and higher-plant PSII. Expand
Glutamate-354 of the CP43 polypeptide interacts with the oxygen-evolving Mn4Ca cluster of photosystem II: a preliminary characterization of the Glu354Gln mutant
TLDR
The intensities of the mutant EPR and FTIR difference spectra are much greater than the O2 signals and suggest that CP43-Glu354Gln PSII reaction centres are heterogeneous, with a minority fraction able to evolve O2 with normal O2 release kinetics and a majority fraction unable to advance beyond the S2 or S3 states. Expand
Participation of glutamate-333 of the D1 polypeptide in the ligation of the Mn₄CaO₅ cluster in photosystem II.
TLDR
It is concluded that fully functional Mn₄CaO₅ clusters assemble in the presence of the D1-E333Q mutation but that the mutation decreases the yield of assembled clusters and alters the H-bonding properties of one or more water molecules or hydroxide groups that are located on or near the MnℓCaO ₅ cluster. Expand
Cryo-EM Structure of Monomeric Photosystem II from Synechocystis sp. PCC 6803 Lacking the Water-Oxidation Complex
Summary The photosystem II (PSII) enzyme provides nearly all the oxygen on Earth by catalyzing water oxidation via its oxygen-evolving complex (OEC), a heterocubane metal cluster in the PSII activeExpand
Quantum mechanics/molecular mechanics structural models of the oxygen-evolving complex of photosystem II.
TLDR
The resulting computational structural models suggest the complete ligation of the catalytic center by amino acid residues, water, hydroxide and chloride, as determined from the intrinsic electronic properties of the oxomanganese core and the perturbational influence of the surrounding protein environment. Expand
Evidence from FTIR difference spectroscopy of an extensive network of hydrogen bonds near the oxygen-evolving Mn(4)Ca cluster of photosystem II involving D1-Glu65, D2-Glu312, and D1-Glu329.
TLDR
Analyses of the refined X-ray crystallographic structures of photosystem II have revealed the presence of possible channels for the removal of protons from the catalytic Mn(4)Ca cluster during the water-splitting reaction, and a negative band at 1747 cm(-1) was probed. Expand
Expression, assembly and auxiliary functions of photosystem II oxygen-evolving proteins in higher plants
TLDR
The oxygen-evolving complex (OEC) of higher plant photosystem II (PSII) consists of an inorganic Mn4Ca cluster and three nuclear-encoded proteins, PsbO,PsbP and PsbQ, and the role of the small intrinsic PSII proteins is focused on. Expand
Effects of ammonia on the structure of the oxygen-evolving complex in photosystem II as revealed by light-induced FTIR difference spectroscopy.
TLDR
The results suggest that NH(3) induced a significant alteration on the core structure of the Mn(4)CaO(5) cluster in PSII. Expand
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