000044314 001__ 44314
000044314 005__ 20200610184718.0
000044314 0247_ $$2Handle$$a2128/83
000044314 0247_ $$2URI$$a83
000044314 037__ $$aPreJuSER-44314
000044314 0881_ $$aJuel-3969
000044314 088__ $$2JUEL$$aJuel-3969
000044314 1001_ $$0P:(DE-Juel1)VDB584$$aHeitbrink, Dirk$$b0$$eCorresponding author$$uFZJ
000044314 245__ $$aInfrarotspektroskopische Untersuchungen zum Mechanismus der Cytochrom-c-Oxidase
000044314 260__ $$aJülich$$bForschungszentrum Jülich GmbH Zentralbibliothek, Verlag$$c2002
000044314 300__ $$aII, 114 p.
000044314 3367_ $$0PUB:(DE-HGF)11$$2PUB:(DE-HGF)$$aDissertation / PhD Thesis
000044314 3367_ $$0PUB:(DE-HGF)3$$2PUB:(DE-HGF)$$aBook
000044314 3367_ $$02$$2EndNote$$aThesis
000044314 3367_ $$2DRIVER$$adoctoralThesis
000044314 3367_ $$2BibTeX$$aPHDTHESIS
000044314 3367_ $$2DataCite$$aOutput Types/Dissertation
000044314 3367_ $$2ORCID$$aDISSERTATION
000044314 4900_ $$0PERI:(DE-600)2414853-2$$81344$$aBerichte des Forschungszentrums Jülich$$v3969$$x0944-2952
000044314 502__ $$aDüsseldorf, Univ., Diss., 2002$$bDr. (Univ.)$$cUniv. Düsseldorf$$d2002
000044314 500__ $$aRecord converted from VDB: 12.11.2012
000044314 520__ $$aCytochrome c oxidase is a complex biological machinery, which couples the reduction of oxygen to a vectorial transport of protons across the membrane. To achieve this, the protein takes up eight protons, four electrons, and an oxygen molecule. The electrons and four of the eight protons are used for the reduction of oxygen to produce water. The remaining four protons are pumped across the membrane. In this work, Fourier-transorm infrared spectroscopy was applied to provide insight into the structural and functional relationships of the complex catalytic cycle. To accomplish this, different strategies were applied: The results obtained with the $\textit{fully reduced}$, CO-bound cytochrome c oxidase from bovine heart showed for the first time the possibility of performing difference spectroscopy on this enzyme with a time-resolution of 5 $\mu$s in the range of 2200 to 950 cm$^{-1}$. The evaluation of the data revealed a dynamic link between the transient binding of CO to Cu$_{B}$ and the movement of an amino acid side chain (E286) approximately 12 $\mathring{A}$ away. This amino acid is part of the D-channel and thought to play an important role in guiding the protons either into the binuclear center or through the membrane. The results presented in this work suggest a mechanism in which oxygen binding is controlled via E286. The outcome of the measurements with the $\textit{two electron-reduced}$, CO-bound cytochrome c oxidase from $\textit{Rhodobacter sphaeroides}$ indicate the deprotonation of E286 during electron transfer from heme a$_{3}$ to heme a. This result contradicts the current model of the catalytic-cycle because this deprotonation suggests an uptake of just one proton rather than two through the K-channel. Redox difference spectra of wild type and mutant cytochrome c oxidase obtained with the attenuated total reflection technique pointed out the precise assignment of a band feature. This signal was clearly attributed to a conformational change of the side chain of amino acid E286. For the first time it was possible to record a difference spectrum in the IR of the oxidative part of the catalytic cycle. The F $\textit{minus}$ O spectrum showed an involvement of a tyrosine which undergoes deprotonation.
000044314 536__ $$0G:(DE-Juel1)FUEK96$$2G:(DE-HGF)$$aBiologische Strukturforschung$$c42.50.0$$x0
000044314 655_7 $$aHochschulschrift$$xDissertation (Univ.)
000044314 8564_ $$uhttps://juser.fz-juelich.de/record/44314/files/Juel_3969_Heitbrink.pdf$$yOpenAccess
000044314 909CO $$ooai:juser.fz-juelich.de:44314$$pdnbdelivery$$pVDB$$pdriver$$popen_access$$popenaire
000044314 915__ $$0StatID:(DE-HGF)0510$$2StatID$$aOpenAccess
000044314 9141_ $$y2001
000044314 9131_ $$0G:(DE-Juel1)FUEK96$$bLebenswissenschaften$$k42.50.0$$lBiologische Informationsverarbeitung$$vBiologische Strukturforschung$$x0
000044314 9201_ $$0I:(DE-Juel1)VDB58$$d31.12.2006$$gIBI$$kIBI-2$$lBiologische Strukturforschung$$x0
000044314 970__ $$aVDB:(DE-Juel1)6403
000044314 9801_ $$aFullTexts
000044314 980__ $$aVDB
000044314 980__ $$aJUWEL
000044314 980__ $$aConvertedRecord
000044314 980__ $$aphd
000044314 980__ $$aI:(DE-Juel1)ISB-2-20090406
000044314 980__ $$aUNRESTRICTED
000044314 980__ $$aI:(DE-Juel1)ICS-6-20110106
000044314 980__ $$aFullTexts
000044314 981__ $$aI:(DE-Juel1)IBI-7-20200312
000044314 981__ $$aI:(DE-Juel1)ISB-2-20090406
000044314 981__ $$aI:(DE-Juel1)ICS-6-20110106