Hauptseite > Publikationsdatenbank > Direct Observation of Protonation Reactions during the Catalytic Cycle of Cytochrome c Oxidase > print

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005     20200423203554.0
017 _ _ |a This version is available at http://www.pnas.org, http://dx.doi.org/10.1073/pnas.1530408100
024 7 _ |a pmid:12851460
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024 7 _ |a pmc:PMC166378
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024 7 _ |a 10.1073/pnas.1530408100
|2 DOI
024 7 _ |a WOS:000184371000024
|2 WOS
024 7 _ |a 2128/2650
|2 Handle
037 _ _ |a PreJuSER-32452
041 _ _ |a eng
082 _ _ |a 000
084 _ _ |2 WoS
|a Multidisciplinary Sciences
100 1 _ |a Nyquist, R.
|b 0
|0 P:(DE-HGF)0
245 _ _ |a Direct Observation of Protonation Reactions during the Catalytic Cycle of Cytochrome c Oxidase
260 _ _ |a Washington, DC
|b Academy
|c 2003
300 _ _ |a 8715 - 8720
336 7 _ |a Journal Article
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336 7 _ |a Journal Article
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336 7 _ |a ARTICLE
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336 7 _ |a JOURNAL_ARTICLE
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336 7 _ |a article
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440 _ 0 |a Proceedings of the National Academy of Sciences of the United States of America
|x 0027-8424
|0 5100
|v 100
500 _ _ |a Record converted from VDB: 12.11.2012
520 _ _ |a Cytochrome c oxidase, the terminal protein in the respiratory chain, converts oxygen into water and helps generate the electrochemical gradient used in the synthesis of ATP. The catalytic action of cytochrome c oxidase involves electron transfer, proton transfer, and O2 reduction. These events trigger specific molecular changes at the active site, which, in turn, influence changes throughout the protein, including alterations of amino acid side chain orientations, hydrogen bond patterns, and protonation states. We have used IR difference spectroscopy to investigate such modulations for the functional intermediate states E, R2,Pm, and F. These spectra reveal deprotonation of its key glutamic acid E286 in the E and in the Pm states. The consecutive deprotonation and reprotonation of E286 twice within one catalytic turnover illustrates the role of this residue as a proton shuttle. In addition, the spectra point toward deprotonation of a redox-active tyrosine, plausibly Y288, in the F intermediate. Structural insights into the molecular mechanism of catalysis based on the subtle molecular changes observed with IR difference spectroscopy are discussed.
536 _ _ |a Neurowissenschaften
|c L01
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588 _ _ |a Dataset connected to Web of Science, Pubmed
650 _ 2 |2 MeSH
|a Biophysical Phenomena
650 _ 2 |2 MeSH
|a Biophysics
650 _ 2 |2 MeSH
|a Carbon Monoxide: chemistry
650 _ 2 |2 MeSH
|a Catalysis
650 _ 2 |2 MeSH
|a Electron Transport
650 _ 2 |2 MeSH
|a Electron Transport Complex IV: chemistry
650 _ 2 |2 MeSH
|a Electron Transport Complex IV: genetics
650 _ 2 |2 MeSH
|a Electron Transport Complex IV: metabolism
650 _ 2 |2 MeSH
|a Glutamic Acid: chemistry
650 _ 2 |2 MeSH
|a Models, Molecular
650 _ 2 |2 MeSH
|a Mutagenesis, Site-Directed
650 _ 2 |2 MeSH
|a Oxidation-Reduction
650 _ 2 |2 MeSH
|a Protein Conformation
650 _ 2 |2 MeSH
|a Protons
650 _ 2 |2 MeSH
|a Rhodobacter sphaeroides: enzymology
650 _ 2 |2 MeSH
|a Rhodobacter sphaeroides: genetics
650 _ 2 |2 MeSH
|a Spectrophotometry, Infrared
650 _ 7 |0 0
|2 NLM Chemicals
|a Protons
650 _ 7 |0 56-86-0
|2 NLM Chemicals
|a Glutamic Acid
650 _ 7 |0 630-08-0
|2 NLM Chemicals
|a Carbon Monoxide
650 _ 7 |0 EC 1.9.3.1
|2 NLM Chemicals
|a Electron Transport Complex IV
650 _ 7 |a J
|2 WoSType
653 2 0 |2 Author
|a electron transfer
653 2 0 |2 Author
|a infrared attenuated total reflection
653 2 0 |2 Author
|a membrane protein
653 2 0 |2 Author
|a bacteriorhodopsis
653 2 0 |2 Author
|a glutamic acid
700 1 _ |a Heitbrink, D.
|b 1
|0 P:(DE-HGF)0
700 1 _ |a Bolwien, C.
|b 2
|0 P:(DE-HGF)0
700 1 _ |a Wells, T. A.
|b 3
|0 P:(DE-HGF)0
700 1 _ |a Gennis, R. B.
|b 4
|0 P:(DE-HGF)0
700 1 _ |a Heberle, J.
|b 5
|u FZJ
|0 P:(DE-Juel1)VDB572
773 _ _ |a 10.1073/pnas.1530408100
|g Vol. 100, p. 8715 - 8720
|p 8715 - 8720
|q 100<8715 - 8720
|0 PERI:(DE-600)1461794-8
|t Proceedings of the National Academy of Sciences of the United States of America
|v 100
|y 2003
|x 0027-8424
856 7 _ |2 Pubmed Central
|u http://www.ncbi.nlm.nih.gov/pmc/articles/PMC166378
856 4 _ |u https://juser.fz-juelich.de/record/32452/files/34684.pdf
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