000032452 001__ 32452
000032452 005__ 20200423203554.0
000032452 017__ $$aThis version is available at http://www.pnas.org, http://dx.doi.org/10.1073/pnas.1530408100
000032452 0247_ $$2pmid$$apmid:12851460
000032452 0247_ $$2pmc$$apmc:PMC166378
000032452 0247_ $$2DOI$$a10.1073/pnas.1530408100
000032452 0247_ $$2WOS$$aWOS:000184371000024
000032452 0247_ $$2Handle$$a2128/2650
000032452 037__ $$aPreJuSER-32452
000032452 041__ $$aeng
000032452 082__ $$a000
000032452 084__ $$2WoS$$aMultidisciplinary Sciences
000032452 1001_ $$0P:(DE-HGF)0$$aNyquist, R.$$b0
000032452 245__ $$aDirect Observation of Protonation Reactions during the Catalytic Cycle of Cytochrome c Oxidase
000032452 260__ $$aWashington, DC$$bAcademy$$c2003
000032452 300__ $$a8715 - 8720
000032452 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
000032452 3367_ $$2DataCite$$aOutput Types/Journal article
000032452 3367_ $$00$$2EndNote$$aJournal Article
000032452 3367_ $$2BibTeX$$aARTICLE
000032452 3367_ $$2ORCID$$aJOURNAL_ARTICLE
000032452 3367_ $$2DRIVER$$aarticle
000032452 440_0 $$05100$$aProceedings of the National Academy of Sciences of the United States of America$$v100$$x0027-8424
000032452 500__ $$aRecord converted from VDB: 12.11.2012
000032452 520__ $$aCytochrome 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.
000032452 536__ $$0G:(DE-Juel1)FUEK255$$2G:(DE-HGF)$$aNeurowissenschaften$$cL01$$x0
000032452 588__ $$aDataset connected to Web of Science, Pubmed
000032452 650_2 $$2MeSH$$aBiophysical Phenomena
000032452 650_2 $$2MeSH$$aBiophysics
000032452 650_2 $$2MeSH$$aCarbon Monoxide: chemistry
000032452 650_2 $$2MeSH$$aCatalysis
000032452 650_2 $$2MeSH$$aElectron Transport
000032452 650_2 $$2MeSH$$aElectron Transport Complex IV: chemistry
000032452 650_2 $$2MeSH$$aElectron Transport Complex IV: genetics
000032452 650_2 $$2MeSH$$aElectron Transport Complex IV: metabolism
000032452 650_2 $$2MeSH$$aGlutamic Acid: chemistry
000032452 650_2 $$2MeSH$$aModels, Molecular
000032452 650_2 $$2MeSH$$aMutagenesis, Site-Directed
000032452 650_2 $$2MeSH$$aOxidation-Reduction
000032452 650_2 $$2MeSH$$aProtein Conformation
000032452 650_2 $$2MeSH$$aProtons
000032452 650_2 $$2MeSH$$aRhodobacter sphaeroides: enzymology
000032452 650_2 $$2MeSH$$aRhodobacter sphaeroides: genetics
000032452 650_2 $$2MeSH$$aSpectrophotometry, Infrared
000032452 650_7 $$00$$2NLM Chemicals$$aProtons
000032452 650_7 $$056-86-0$$2NLM Chemicals$$aGlutamic Acid
000032452 650_7 $$0630-08-0$$2NLM Chemicals$$aCarbon Monoxide
000032452 650_7 $$0EC 1.9.3.1$$2NLM Chemicals$$aElectron Transport Complex IV
000032452 650_7 $$2WoSType$$aJ
000032452 65320 $$2Author$$aelectron transfer
000032452 65320 $$2Author$$ainfrared attenuated total reflection
000032452 65320 $$2Author$$amembrane protein
000032452 65320 $$2Author$$abacteriorhodopsis
000032452 65320 $$2Author$$aglutamic acid
000032452 7001_ $$0P:(DE-HGF)0$$aHeitbrink, D.$$b1
000032452 7001_ $$0P:(DE-HGF)0$$aBolwien, C.$$b2
000032452 7001_ $$0P:(DE-HGF)0$$aWells, T. A.$$b3
000032452 7001_ $$0P:(DE-HGF)0$$aGennis, R. B.$$b4
000032452 7001_ $$0P:(DE-Juel1)VDB572$$aHeberle, J.$$b5$$uFZJ
000032452 773__ $$0PERI:(DE-600)1461794-8$$a10.1073/pnas.1530408100$$gVol. 100, p. 8715 - 8720$$p8715 - 8720$$q100<8715 - 8720$$tProceedings of the National Academy of Sciences of the United States of America$$v100$$x0027-8424$$y2003
000032452 8567_ $$2Pubmed Central$$uhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC166378
000032452 8564_ $$uhttps://juser.fz-juelich.de/record/32452/files/34684.pdf$$yOpenAccess
000032452 8564_ $$uhttps://juser.fz-juelich.de/record/32452/files/34684.jpg?subformat=icon-1440$$xicon-1440$$yOpenAccess
000032452 8564_ $$uhttps://juser.fz-juelich.de/record/32452/files/34684.jpg?subformat=icon-180$$xicon-180$$yOpenAccess
000032452 8564_ $$uhttps://juser.fz-juelich.de/record/32452/files/34684.jpg?subformat=icon-640$$xicon-640$$yOpenAccess
000032452 909CO $$ooai:juser.fz-juelich.de:32452$$pdnbdelivery$$pVDB$$pdriver$$popen_access$$popenaire
000032452 9131_ $$0G:(DE-Juel1)FUEK255$$bLeben$$kL01$$lFunktion und Dysfunktion des Nervensystems$$vNeurowissenschaften$$x0
000032452 9141_ $$y2003
000032452 915__ $$0StatID:(DE-HGF)0010$$aJCR/ISI refereed
000032452 915__ $$0StatID:(DE-HGF)0510$$2StatID$$aOpenAccess
000032452 9201_ $$0I:(DE-Juel1)VDB58$$d31.12.2006$$gIBI$$kIBI-2$$lBiologische Strukturforschung$$x0
000032452 970__ $$aVDB:(DE-Juel1)34684
000032452 9801_ $$aFullTexts
000032452 980__ $$aVDB
000032452 980__ $$aJUWEL
000032452 980__ $$aConvertedRecord
000032452 980__ $$ajournal
000032452 980__ $$aI:(DE-Juel1)ISB-2-20090406
000032452 980__ $$aUNRESTRICTED
000032452 980__ $$aI:(DE-Juel1)ICS-6-20110106
000032452 980__ $$aFullTexts
000032452 981__ $$aI:(DE-Juel1)IBI-7-20200312
000032452 981__ $$aI:(DE-Juel1)ISB-2-20090406
000032452 981__ $$aI:(DE-Juel1)ICS-6-20110106