GLORIA

GEOMAR Library Ocean Research Information Access

Language
Preferred search index
Number of Hits per Page
Default Sort Criterion
Default Sort Ordering
Size of Search History
Default Email Address
Default Export Format
Default Export Encoding
Facet list arrangement
Maximum number of values per filter
Auto Completion
Topics (search only within journals and journal articles that belong to one or more of the selected topics)
Feed Format
Maximum Number of Items per Feed

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
Filter
  • Seibert, Michael  (2)
  • Linguistics  (2)
  • 1
    Online Resource
    Online Resource
    Proceedings of the National Academy of Sciences ; 1989
    In:  Proceedings of the National Academy of Sciences Vol. 86, No. 2 ( 1989-01), p. 524-528
    In: Proceedings of the National Academy of Sciences, Proceedings of the National Academy of Sciences, Vol. 86, No. 2 ( 1989-01), p. 524-528
    Abstract: We have measured directly the rate of formation of the oxidized chlorophyll a electron donor (P680 + ) and the reduced electron acceptor pheophytin a - (Pheo a - ) following excitation of isolated spinach photosystem II reaction centers at 4°C. The reaction-center complex consists of D 1 , D 2 , and cytochrome b -559 proteins and was prepared by a procedure that stabilizes the protein complex. Transient absorption difference spectra were measured from 440 to 850 nm as a function of time with 500-fs resolution following 610-nm laser excitation. The formation of P680 + -Pheo a - is indicated by the appearance of a band due to P680 + at 820 nm and corresponding absorbance changes at 505 and 540 nm due to formation of Pheo a - . The appearance of the 820-nm band is monoexponential with τ = 3.0 ± 0.6 ps. The time constant for decay of 1* P680, the lowest excited singlet state of P680, monitored at 650 nm, is τ = 2.6 ± 0.6 ps and agrees with that of the appearance of P680 + within experimental error. Treatment of the photosystem II reaction centers with sodium dithionite and methyl viologen followed by exposure to laser excitation, conditions known to result in accumulation of Pheo a - , results in formation of a transient absorption spectrum due to 1* P680. We find no evidence for an electron acceptor that precedes the formation of Pheo a - .
    Type of Medium: Online Resource
    ISSN: 0027-8424 , 1091-6490
    RVK:
    RVK:
    Language: English
    Publisher: Proceedings of the National Academy of Sciences
    Publication Date: 1989
    detail.hit.zdb_id: 209104-5
    detail.hit.zdb_id: 1461794-8
    SSG: 11
    SSG: 12
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
  • 2
    Online Resource
    Online Resource
    Proceedings of the National Academy of Sciences ; 2002
    In:  Proceedings of the National Academy of Sciences Vol. 99, No. 6 ( 2002-03-19), p. 4091-4096
    In: Proceedings of the National Academy of Sciences, Proceedings of the National Academy of Sciences, Vol. 99, No. 6 ( 2002-03-19), p. 4091-4096
    Abstract: The peripheral accessory chlorophylls (Chls) of the photosystem II (PSII) reaction center (RC) are coordinated by a pair of symmetry-related histidine residues (D1-H118 and D2-H117). These Chls participate in energy transfer from the proximal antennae complexes (CP43 and CP47) to the RC core chromophores. In addition, one or both of the peripheral Chls are redox-active and participate in a low-quantum-yield electron transfer cycle around PSII. We demonstrate that conservative mutations of the D2-H117 residue result in decreased Chl fluorescence quenching efficiency attributed to reduced accumulation of the peripheral accessory Chl cation, Chl \documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \setlength{\oddsidemargin}{-69pt} \begin{document} \begin{equation*}{\mathrm{_{Z}^{+}}}\end{equation*}\end{document} . In contrast, identical symmetry-related mutations at residue D1-H118 had no effect on Chl fluorescence yield or quenching kinetics. Mutagenesis of the D2-H117 residue also altered the line width of the Chl \documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \setlength{\oddsidemargin}{-69pt} \begin{document} \begin{equation*}{\mathrm{_{Z}^{+}}}\end{equation*}\end{document} EPR signal, but the line shape of the D1-H118Q mutant remained unchanged. The D1-H118 and D2-H117 mutations also altered energy transfer properties in PSII RCs. Unlike wild type or the D1-H118Q mutant, D2-H117N RCs exhibited a reduced CD doublet in the red region of Chl absorbance band, indicative of reduced energetic coupling between P680 and the peripheral accessory Chl. In addition, transient absorption measurements of D2-H117N RCs, excited on the blue side of the Chl absorbance band, exhibited a (≈400 fs) pheophytin Q X band bleach lifetime component not seen in wild-type or D1-H118Q RCs. The origin of this component may be related to delayed fast-energy equilibration of the excited state between the core pigments of this mutant.
    Type of Medium: Online Resource
    ISSN: 0027-8424 , 1091-6490
    RVK:
    RVK:
    Language: English
    Publisher: Proceedings of the National Academy of Sciences
    Publication Date: 2002
    detail.hit.zdb_id: 209104-5
    detail.hit.zdb_id: 1461794-8
    SSG: 11
    SSG: 12
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...