EPR spectroscopy of the manganese cluster of photosystem II

Haddy, Alice

doi:10.1007/s11120-007-9194-9

Cited by 117 publications

(128 citation statements)

References 108 publications

Supporting

Mentioning

127

Contrasting

Order By: Relevance

“…For example, the S 3 state parallel mode EPR signal (Matsukawa et al 1999) and the g = 4.1 perpendicular mode S 2 state EPR signal (for review see, Haddy 2007) cannot be observed in presence of methanol or ethanol, while in PSII membrane fragments from higher plants the S 0 multiline signal can only be resolved after methanol addition (Messinger et al 1997a). An ESEEM study employing 2 H-labeled methanol clearly showed that methanol (and ethanol) binds at-or at least very close to-the Mn 4 O x Ca cluster (Force et al 1998).…”

Section: Introductionmentioning

confidence: 99%

“…Several EPR and FTIR studies suggest that ammonia has one or two binding sites at the Mn 4 O x Ca cluster (for review see, Debus 1992;Hillier and Messinger 2005). At high enough concentrations ammonia inhibits O 2 evolution and alters the S 2 state EPR multiline signal (Haddy 2007). The possible competition between ammonia and methanol for binding sites at the water-splitting Mn 4 O x Ca cluster of photosystem II has been studied by two groups.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Effects of methanol on the S i -state transitions in photosynthetic water-splitting

Nöring¹,

Shevela

Ренгер

et al. 2008

Photosynth Res

View full text Add to dashboard Cite

From a chemical point of view methanol is one of the closest analogues of water. Consistent with this idea EPR spectroscopy studies have shown that methanol binds at-or at least very close to-the Mn 4 O x Ca cluster of photosystem II (PSII). In contrast, Clark-type oxygen rate measurements demonstrate that the O 2 evolving activity of PSII is surprisingly unaffected by methanol concentrations of up to 10%. Here we study for the first time in detail the effect of methanol on photosynthetic water-splitting by employing a Joliot-type bare platinum electrode. We demonstrate a linear dependence of the miss parameter for S i state advancement on the methanol concentrations in the range of 0-10% (v/v). This finding is consistent with the idea that methanol binds in PSII with similar affinity as water to one or both substrate binding sites at the Mn 4 O x Ca cluster. The possibility is discussed that the two substrate water molecules bind at different stages of the cycle, one during the S 4 ? S 0 and the other during the S 2 ? S 3 transition.

show abstract

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Effects of methanol on the S i -state transitions in photosynthetic water-splitting

Nöring¹,

Shevela

Ренгер

et al. 2008

Photosynth Res

View full text Add to dashboard Cite

show abstract

“…However, due to the limited knowledge about the accurate geometry of the Mn 4 Ca cluster, a direct correlation of the spec-troscopic data to structural changes of the cluster is difficult. The recent high resolution crystal structure from XRD reported by Umena et al (1) has provided a more precise geometry of the OEC structure with possibly limited effects from radiation damage (see below).…”

mentioning

confidence: 99%

Structural Changes of the Oxygen-evolving Complex in Photosystem II during the Catalytic Cycle

Glöckner

Kern

Broser

et al. 2013

Journal of Biological Chemistry

152

197

View full text Add to dashboard Cite

Background: Mn 4 CaO 5 cluster catalyzes water oxidation in photosystem II. Results: Mn-Mn/Ca/ligand distances and changes in the structure of the Mn 4 CaO 5 cluster are determined for the intermediate states in the reaction using x-ray spectroscopy. Conclusion: Position of one bridging oxygen and related geometric changes may be critical during catalysis. Significance: Knowledge about structural changes during catalysis is crucial for understanding the O-O bond formation mechanism in PSII.

show abstract

“…Not only is this radiation damage a problem for PSII, but it also presents a challenge encountered in many other redox-active metalloenzymes [15][16][17][18]. Thus far, the geometric and electronic structural information of the intact Mn 4 CaO 5 cluster has been primarily addressed by spectroscopic methods [19][20][21][22], especially X-ray absorption (XAS) and emission spectroscopy (XES) techniques [14,[23][24][25]. Among these, XES is a powerful method for studying the charge and spin density and the ligand environment of the metal sites [26].…”

Section: Introductionmentioning

confidence: 99%

The Mn ₄ Ca photosynthetic water-oxidation catalyst studied by simultaneous X-ray spectroscopy and crystallography using an X-ray free-electron laser

Tran

Kern

Hattne

et al. 2014

Phil. Trans. R. Soc. B

View full text Add to dashboard Cite

ReviewCite this article: Tran R et al. 2014 The Mn 4 Ca photosynthetic water-oxidation catalyst studied by simultaneous X-ray spectroscopy and crystallography using an X-ray free-electron laser. Phil. Trans. R. Soc. B 369: 20130324. http://dx.doi.org/10.1098/rstb.2013.0324One contribution of 27 to a Discussion Meeting Issue 'Biology with free-electron X-ray lasers'.Subject Areas: biophysics, plant science, structural biology Keywords: manganese, oxygen-evolving complex, photosystem II, X-ray crystallography, X-ray emission spectroscopy, X-ray free-electron laser Author for correspondence: Vittal K. Yachandra e-mail: vkyachandra@lbl.govThe Mn 4 Ca photosynthetic wateroxidation catalyst studied by simultaneous X-ray spectroscopy and crystallography using an X-ray free-electron laser The structure of photosystem II and the catalytic intermediate states of the Mn 4 CaO 5 cluster involved in water oxidation have been studied intensively over the past several years. An understanding of the sequential chemistry of light absorption and the mechanism of water oxidation, however, requires a new approach beyond the conventional steady-state crystallography and X-ray spectroscopy at cryogenic temperatures. In this report, we present the preliminary progress using an X-ray free-electron laser to determine simultaneously the light-induced protein dynamics via crystallography and the local chemistry that occurs at the catalytic centre using X-ray spectroscopy under functional conditions at room temperature.

show abstract

EPR spectroscopy of the manganese cluster of photosystem II

Cited by 117 publications

References 108 publications

Effects of methanol on the S i -state transitions in photosynthetic water-splitting

Effects of methanol on the S i -state transitions in photosynthetic water-splitting

Structural Changes of the Oxygen-evolving Complex in Photosystem II during the Catalytic Cycle

The Mn ₄ Ca photosynthetic water-oxidation catalyst studied by simultaneous X-ray spectroscopy and crystallography using an X-ray free-electron laser

Contact Info

Product

Resources

About