Energetics of proton transfer pathways in reaction centers from Rhodobacter sphaeroides. The Glu-H173 activated mutants (Q45214716)

10 December 2017

title

Energetics of proton transfer pathways in reaction centers from Rhodobacter sphaeroides. The Glu-H173 activated mutants (English)

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10 December 2017

main subject

Rhodobacter sphaeroides

object named as

Rhodobacter sphaeroides

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1

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10 December 2017

2

Ernst-Walter Knapp

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10 December 2017

language of work or name

English

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publication date

6 January 2005

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Journal of Biological Chemistry

10 December 2017

number of pages

5

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based on heuristic

inferred from page(s)

published in

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10 December 2017

volume

280

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10 December 2017

issue

13

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10 December 2017

page(s)

12446-12450

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Simultaneous replacement of Asp-L210 and Asp-M17 with Asn increases proton uptake by Glu-L212 upon first electron transfer to QB in reaction centers from Rhodobacter sphaeroides

10 December 2017

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Pathway of proton transfer in bacterial reaction centers: second-site mutation Asn-M44-->Asp restores electron and proton transfer in reaction centers from the photosynthetically deficient Asp-L213-->Asn mutant of Rhodobacter sphaeroides

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Mechanism of proton transfer inhibition by Cd(2+) binding to bacterial reaction centers: determination of the pK(A) of functionally important histidine residues

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X-Ray structure determination of three mutants of the bacterial photosynthetic reaction centers from Rb. sphaeroides; altered proton transfer pathways

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A new metal-binding site in photosynthetic bacterial reaction centers that modulates QA to QB electron transfer

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Identification of the proton pathway in bacterial reaction centers: inhibition of proton transfer by binding of Zn2+ or Cd2+.

21 January 2018

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Determination of the binding sites of the proton transfer inhibitors Cd2+ and Zn2+ in bacterial reaction centers

21 January 2018

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Identification of the proton pathway in bacterial reaction centers: decrease of proton transfer rate by mutation of surface histidines at H126 and H128 and chemical rescue by imidazole identifies the initial proton donors

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Retardation of proton transfer caused by binding of the transition metal ion to the bacterial reaction center is due to pKa shifts of key protonatable residues

21 January 2018

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Redox potential of quinones in photosynthetic reaction centers from Rhodobacter sphaeroides: dependence on protonation of Glu-L212 and Asp-L213.

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Protonation of Glu L212 following QB- formation in the photosynthetic reaction center of Rhodobacter sphaeroides: evidence from time-resolved infrared spectroscopy

21 January 2018

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21 January 2018

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Proton uptake by carboxylic acid groups upon photoreduction of the secondary quinone (QB) in bacterial reaction centers from Rhodobacter sphaeroides: FTIR studies on the effects of replacing Glu H173.

21 January 2018

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21 January 2018

Protons forge new paths.

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Identification of the proton pathway in bacterial reaction centers: cooperation between Asp-M17 and Asp-L210 facilitates proton transfer to the secondary quinone (QB).

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Pathway of proton transfer in bacterial reaction centers: replacement of glutamic acid 212 in the L subunit by glutamine inhibits quinone (secondary acceptor) turnover

21 January 2018

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Calculated protein and proton motions coupled to electron transfer: electron transfer from QA- to QB in bacterial photosynthetic reaction centers.

21 January 2018

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Effect of binding of Cd2+ on bacterial reaction center mutants: proton-transfer uses interdependent pathways

21 January 2018

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Site-specific and compensatory mutations imply unexpected pathways for proton delivery to the QB binding site of the photosynthetic reaction center

21 January 2018

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Architecture of the photosynthetic oxygen-evolving center

21 January 2018

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Tuning electron transfer by ester-group of chlorophylls in bacterial photosynthetic reaction center

21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.M413531200

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10 December 2017

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