Mid- to low-frequency Fourier transform infrared spectra of S-state cycle for photosynthetic water oxidation in Synechocystis sp. PCC 6803.

  title={Mid- to low-frequency Fourier transform infrared spectra of S-state cycle for photosynthetic water oxidation in Synechocystis sp. PCC 6803.},
  author={T. Yamanari and Y. Kimura and N. Mizusawa and A. Ishii and T. Ono},
  volume={43 23},
Flash-induced Fourier transform infrared (FTIR) difference spectra for the four-step S-state cycle and the effects of global (15)N- and (13)C-isotope labeling on the difference spectra were examined for the first time in the mid- to low-frequency (1200-800 cm(-1)) as well as the mid-frequency (1700-1200 cm(-1)) regions using photosystem (PS) II core particles from cyanobacterium Synechocystis sp. PCC 6803. The difference spectra clearly exhibited the characteristic vibrational features for each… Expand
The Photosynthetic Mn Complex in Its Reaction Cycle: An Attempt to Obtain Pure FTIR Difference Spectra for the Four Transitions Between Semi-Stable S-States and for QB Redox Transitions
In Oxygenic Photosynthesis, Water Is Oxidized At A Mn4Ca Complex Bound To The Proteins Of Photosystem Ii (Psii). The Water-Oxidation Cycle Of The Mn Complex May Involve Nine Distinct States Of The MnExpand
No evidence from FTIR difference spectroscopy that aspartate-342 of the D1 polypeptide ligates a Mn ion that undergoes oxidation during the S0 to S1, S1 to S2, or S2 to S3 transitions in photosystem II.
To determine if D1-Asp342 ligates a Mn ion that undergoes oxidation during one or more of the S0 --> S1, S1 --> S2, and S2 --> S3 transitions, the FTIR difference spectra of the individual S state transitions in D 1-D342N mutant PSII particles from the cyanobacterium Synechocystis sp. Expand
Fourier transform infrared analysis of the photosynthetic oxygen-evolving center
Abstract Fourier transform infrared (FTIR) difference spectroscopy is a powerful method to study the detailed structures of active sites in enzymes. It can detect basically all molecules involved inExpand
Structural Changes of D1 C-terminal α-Carboxylate during S-state Cycling in Photosynthetic Oxygen Evolution*
The results indicate that the α-carboxylate of C-terminal Ala-344 is structurally associated with a manganese ion that becomes oxidized upon the S1-to-S2 transition and reduced reversely upon theS3- to-S0 transition but is not associated with manganESE ion(s) oxidized during the S0-to theS1 (and S2-to -S3) transition(s). Expand
Monitoring proton release during photosynthetic water oxidation in photosystem II by means of isotope-edited infrared spectroscopy.
It was concluded that proton release from substrate water takes place with a 1:0:1:2 stoichiometry, which is perturbed by partial protonation/deprotonation of side groups probably of Arg, Lys, or Tyr located nearby the WOC. Expand
Light-induced FTIR difference spectroscopy as a powerful tool toward understanding the molecular mechanism of photosynthetic oxygen evolution
  • T. Noguchi
  • Chemistry, Medicine
  • Photosynthesis Research
  • 2007
FTIR spectra provide extensive structural information on the amino acid side groups, polypeptide chains, metal core, and water molecules, which constitute the OEC and are involved in its reaction, and are thus becoming a powerful tool in investigating the reaction mechanism of photosynthetic oxygen evolution. 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.
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
FTIR evidence that the PsbP extrinsic protein induces protein conformational changes around the oxygen-evolving Mn cluster in photosystem II.
Results indicate that the PsbP protein, but not PsbQ and PsbO, affects the protein conformation in the intrinsic proteins without changing the ligand structure, and the evidence strongly suggests that protein conformational changes around the Mn cluster induced by PsbB affect the binding properties of Ca(2+) and Cl(-) and enhance their retention. Expand
Glutamate-354 of the CP43 polypeptide interacts with the oxygen-evolving Mn4Ca cluster of photosystem II: a preliminary characterization of the Glu354Gln mutant
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
Evidence from FTIR difference spectroscopy that D1-Asp61 influences the water reactions of the oxygen-evolving Mn4CaO5 cluster of photosystem II.
  • R. Debus
  • Chemistry, Medicine
  • Biochemistry
  • 2014
This study characterizes the FTIR properties of the D1-D61A mutant of the cyanobacterium, Synechocystis sp. Expand