Hydrogen bonds involved in binding the Qi-site semiquinone in the bc1 complex, identified through deuterium exchange using pulsed EPR.

Hydrogen bonds involved in binding the Qi-site semiquinone in the bc1 complex, identified through deuterium exchange using pulsed EPR.

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http://www.wikidata.org/entity/Q44737271
Characterization of the semiquinone radical stabilized by the cytochrome aa3-600 menaquinol oxidase of Bacillus subtilisEvolution of cytochrome bc complexes: from membrane-anchored dehydrogenases of ancient bacteria to triggers of apoptosis in vertebratesEnergy conversion, redox catalysis and generation of reactive oxygen species by respiratory complex IStructural and computational analysis of the quinone-binding site of complex II (succinate-ubiquinone oxidoreductase): a mechanism of electron transfer and proton conduction during ubiquinone reductionBinding of the respiratory chain inhibitor antimycin to the mitochondrial bc1 complex: a new crystal structure reveals an altered intramolecular hydrogen-bonding pattern.Hydrogen bonds between nitrogen donors and the semiquinone in the Qi-site of the bc1 complex.The Q-cycle reviewed: How well does a monomeric mechanism of the bc(1) complex account for the function of a dimeric complex?Proton environment of reduced Rieske iron-sulfur cluster probed by two-dimensional ESEEM spectroscopy.Probing the Menasemiquinone Binding Mode to Nitrate Reductase A by Selective 2 H and 15 N Labeling, HYSCORE Spectroscopy, and DFT Modeling.Reaction of superoxide radical with quinone moleculesIdentifying involvement of Lys251/Asp252 pair in electron transfer and associated proton transfer at the quinone reduction site of Rhodobacter capsulatus cytochrome bc1.Determination of the proton environment of high stability Menasemiquinone intermediate in Escherichia coli nitrate reductase A by pulsed EPR.Hydrogen bonding and spin density distribution in the Qb semiquinone of bacterial reaction centers and comparison with the Qa site.Direct evidence for nitrogen ligation to the high stability semiquinone intermediate in Escherichia coli nitrate reductase A.The semiquinone at the Qi site of the bc1 complex explored using HYSCORE spectroscopy and specific isotopic labeling of ubiquinone in Rhodobacter sphaeroides via (13)C methionine and construction of a methionine auxotroph.Semiquinone intermediates are involved in the energy coupling mechanism of E. coli complex I.Cytochrome b6 arginine 214 of Synechococcus sp. PCC 7002, a key residue for quinone-reductase site function and turnover of the cytochrome bf complex.
P2860

Hydrogen bonds involved in binding the Qi-site semiquinone in the bc1 complex, identified through deuterium exchange using pulsed EPR.

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http://www.wikidata.org/entity/Q44737271
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2004 nî lūn-bûn
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Hydrogen bonds involved in bin ...... ium exchange using pulsed EPR.
@en
Hydrogen bonds involved in bin ...... ium exchange using pulsed EPR.
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type
label
Hydrogen bonds involved in bin ...... ium exchange using pulsed EPR.
@en
Hydrogen bonds involved in bin ...... ium exchange using pulsed EPR.
@nl
prefLabel
Hydrogen bonds involved in bin ...... ium exchange using pulsed EPR.
@en
Hydrogen bonds involved in bin ...... ium exchange using pulsed EPR.
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Hydrogen bonds involved in bin ...... ium exchange using pulsed EPR.
@en
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P5875
P698