Untitled

Ridge, Justin P.; Brederode, Marion E. van; Goodwin, Matthew G; Grondelle, Rienk van; Jones, Michael R.

doi:10.1023/a:1006111321083

Cited by 49 publications

(56 citation statements)

References 73 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…This long lifetime indicates stabilization of QB -by this double mutation, in accord with previous observations [35] . In a photoelectrochemical cell, with a mechanism for effective reduction of P + by the working electrode using cyt c as a "wire", such stabilization would be expected to result in photoaccumulation of RCs initially in the state PQB -and, following a second photoexcitation and in the absence of double reduction of QB, the state PQA -QB -.…”

Section: Discussionsupporting

confidence: 92%

“…This mutation causes the RC to assemble without a QA ubiquinone, halting charge separation at the P + HA -state. The AM260W RC has been characterized by a range of spectroscopic techniques [35,44,45], and a 2.1 Å resolution X-ray crystal structure has been determined that showed a lack of a ubiquinone at the QA site and a QB site occupied by UQ10 [36]. In the present study, photoexcitation of purified AM260W RCs failed to produce a change in 865 nm absorbance, indicating a lack of P + formation on a millisecond time scale (Figure 3, black).…”

Section: Qa Binding Site Blocking Mutant Rc Am260wmentioning

confidence: 51%

“…Previous X-ray crystallography and functional studies have shown that substitution of Ala M248 for a much larger Trp residue results in steric exclusion of the QA ubiquinone from its binding pocket [34,35].…”

Section: Structural Characterization Of the Engineered Rcsmentioning

confidence: 99%

“…XbaI-BamHI fragment encompassing the genes for the RC L and M polypeptides [35]. XbaI/BamHI restriction fragments containing the mutations were shuttled into expression vector pRKEH10D [58].…”

Section: Experimental Materialsmentioning

confidence: 99%

See 3 more Smart Citations

On the mechanism of ubiquinone mediated photocurrent generation by a reaction center based photocathode

Friebe¹,

Swainsbury²,

Fyfe³

et al. 2016

Biochimica et Biophysica Acta (BBA) - Bioenergetics

Self Cite

View full text Add to dashboard Cite

Section: Discussionsupporting

confidence: 92%

Section: Qa Binding Site Blocking Mutant Rc Am260wmentioning

confidence: 51%

Section: Structural Characterization Of the Engineered Rcsmentioning

confidence: 99%

Section: Experimental Materialsmentioning

confidence: 99%

See 2 more Smart Citations

On the mechanism of ubiquinone mediated photocurrent generation by a reaction center based photocathode

Friebe¹,

Swainsbury²,

Fyfe³

et al. 2016

Biochimica et Biophysica Acta (BBA) - Bioenergetics

Self Cite

View full text Add to dashboard Cite

“…This residue was mutated to tryptophan with a view to causing exclusion of the Q A ubiquinone and so preventing light-driven transmembrane electron transfer in the reaction center. Spectroscopic studies, a full account of which has been given recently (52), showed that the AM260W reaction center does not possess Q A function, and in particular picosecond time-scale transient absorption spectroscopy showed that light-driven electron transfer is blocked at the state P ϩ H L Ϫ . To characterize further the AM260W reaction center, the complex was purified and crystallized, and x-ray diffraction data were collected according to the procedures described in Methods.…”

Section: Resultsmentioning

confidence: 99%

Structural details of an interaction between cardiolipin and an integral membrane protein

McAuley

Fyfe

Ridge

et al. 1999

Proc. Natl. Acad. Sci. U.S.A.

Self Cite

233

184

View full text Add to dashboard Cite

Anionic lipids play a variety of key roles in biomembrane function, including providing the immediate environment for the integral membrane proteins that catalyze photosynthetic and respiratory energy transduction. Little is known about the molecular basis of these lipid-protein interactions. In this study, x-ray crystallography has been used to examine the structural details of an interaction between cardiolipin and the photoreaction center, a key lightdriven electron transfer protein complex found in the cytoplasmic membrane of photosynthetic bacteria. X-ray diffraction data collected over the resolution range 30.0 -2.1 Å show that binding of the lipid to the protein involves a combination of ionic interactions between the protein and the lipid headgroup and van der Waals interactions between the lipid tails and the electroneutral intramembrane surface of the protein. In the headgroup region, ionic interactions involve polar groups of a number of residues, the protein backbone, and bound water molecules. The lipid tails sit along largely hydrophobic grooves in the irregular surface of the protein. In addition to providing new information on the immediate lipid environment of a key integral membrane protein, this study provides the first, to our knowledge, high-resolution x-ray crystal structure for cardiolipin. The possible significance of this interaction between an integral membrane protein and cardiolipin is considered.

show abstract

A Mechanoresponsive Phase‐Changing Electrolyte Enables Fabrication of High‐Output Solid‐State Photobioelectrochemical Devices from Pigment‐Protein Multilayers

et al. 2017

Self Cite

View full text Add to dashboard Cite

Exploitation of natural photovoltaic reaction center pigment proteins in biohybrid architectures for solar energy harvesting is attractive due to their global abundance, environmental compatibility, and near-unity quantum efficiencies. However, it is challenging to achieve high photocurrents in a device setup due to limitations imposed by low light absorbance by protein monolayers and/or slow long-range diffusion of liquid-phase charge carriers. In an attempt to enhance the photocurrent density achievable by pigment proteins, here, an alternative solid-state device architecture enabled by a mechanoresponsive gel electrolyte that can be applied under nondenaturing conditions is demonstrated. The phase-changing electrolyte gel provides a pervading biocompatible interface for charge conduction through highly absorbing protein multilayers that are fabricated in a simple fashion. Assembled devices exhibit enhanced current stability and a maximal photoresponse of ≈860 µA cm , a fivefold improvement over the best previous comparable devices under standard illumination conditions. Photocurrent generation is enhanced by directional energy transfer through extended layers of light-harvesting complexes, mimicking the modular antenna/transducer architecture of natural photosystems, and by metastable radical pair formation when photovoltaic reaction centers are embedded throughout light-harvesting regions of the device.

show abstract

Untitled

Cited by 49 publications

References 73 publications

On the mechanism of ubiquinone mediated photocurrent generation by a reaction center based photocathode

On the mechanism of ubiquinone mediated photocurrent generation by a reaction center based photocathode

Structural details of an interaction between cardiolipin and an integral membrane protein

A Mechanoresponsive Phase‐Changing Electrolyte Enables Fabrication of High‐Output Solid‐State Photobioelectrochemical Devices from Pigment‐Protein Multilayers

Contact Info

Product

Resources

About