000051337 001__ 51337
000051337 005__ 20200402210131.0
000051337 0247_ $$2pmid$$apmid:16466722
000051337 0247_ $$2DOI$$a10.1016/j.febslet.2006.01.055
000051337 0247_ $$2WOS$$aWOS:000235597700024
000051337 037__ $$aPreJuSER-51337
000051337 041__ $$aeng
000051337 082__ $$a570
000051337 084__ $$2WoS$$aBiochemistry & Molecular Biology
000051337 084__ $$2WoS$$aBiophysics
000051337 084__ $$2WoS$$aCell Biology
000051337 1001_ $$0P:(DE-HGF)0$$aPereira, M. M.$$b0
000051337 245__ $$aA tyrosine residue deprotonates during oxygen reduction by the caa3 reductase from Rhodothermus marinus
000051337 260__ $$aAmsterdam [u.a.]$$bElsevier$$c2006
000051337 300__ $$a1350 - 1354
000051337 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
000051337 3367_ $$2DataCite$$aOutput Types/Journal article
000051337 3367_ $$00$$2EndNote$$aJournal Article
000051337 3367_ $$2BibTeX$$aARTICLE
000051337 3367_ $$2ORCID$$aJOURNAL_ARTICLE
000051337 3367_ $$2DRIVER$$aarticle
000051337 440_0 $$02052$$aFEBS Letters$$v580$$x0014-5793
000051337 500__ $$aRecord converted from VDB: 12.11.2012
000051337 520__ $$aHeme-copper oxygen reductases catalyze proton translocation across the cellular membrane; this takes place during the reaction of oxygen to water. We demonstrate with attenuated total reflection-Fourier transform infrared (ATR-FTIR) difference spectroscopy that a tyrosine residue of the oxygen reductase from the thermohalophilic Rhodothermus marinus becomes deprotonated in the transition from the oxidized state to the catalytic intermediate ferryl state P(M). This tyrosine residue is most probably Y256, the helix VI tyrosine residue proposed to substitute for the D-channel glutamic acid that is absent in this enzyme. Comparison with the mitochondrial like oxygen reductase from Rhodobacter sphaeroides suggests that proton transfer from a strategically situated donor to the active site is a crucial step in the reaction mechanism of oxygen reductases.
000051337 536__ $$0G:(DE-Juel1)FUEK409$$2G:(DE-HGF)$$aFunktion und Dysfunktion des Nervensystems$$cP33$$x0
000051337 588__ $$aDataset connected to Web of Science, Pubmed
000051337 650_2 $$2MeSH$$aBinding Sites
000051337 650_2 $$2MeSH$$aCatalysis
000051337 650_2 $$2MeSH$$aCytochromes a3: metabolism
000051337 650_2 $$2MeSH$$aOxidation-Reduction
000051337 650_2 $$2MeSH$$aOxidoreductases
000051337 650_2 $$2MeSH$$aOxygen: metabolism
000051337 650_2 $$2MeSH$$aProtons
000051337 650_2 $$2MeSH$$aRhodobacter sphaeroides: enzymology
000051337 650_2 $$2MeSH$$aRhodothermus: enzymology
000051337 650_2 $$2MeSH$$aRhodothermus: metabolism
000051337 650_2 $$2MeSH$$aSpectroscopy, Fourier Transform Infrared
000051337 650_2 $$2MeSH$$aTyrosine: chemistry
000051337 650_7 $$00$$2NLM Chemicals$$aCytochromes a3
000051337 650_7 $$00$$2NLM Chemicals$$aProtons
000051337 650_7 $$055520-40-6$$2NLM Chemicals$$aTyrosine
000051337 650_7 $$07782-44-7$$2NLM Chemicals$$aOxygen
000051337 650_7 $$0EC 1.-$$2NLM Chemicals$$aOxidoreductases
000051337 650_7 $$2WoSType$$aJ
000051337 65320 $$2Author$$aFTIR
000051337 65320 $$2Author$$avibrational spectroscopy
000051337 65320 $$2Author$$acytochrome c
000051337 65320 $$2Author$$aoxidase
000051337 65320 $$2Author$$arespiration
000051337 65320 $$2Author$$aproton translocation
000051337 65320 $$2Author$$aelectron transfer
000051337 65320 $$2Author$$aglutamic acid
000051337 65320 $$2Author$$atyrosine
000051337 65320 $$2Author$$amembrane
000051337 65320 $$2Author$$abacteriorhodopsin
000051337 7001_ $$0P:(DE-HGF)0$$aSousa, F. L.$$b1
000051337 7001_ $$0P:(DE-HGF)0$$aTeixeira, M.$$b2
000051337 7001_ $$0P:(DE-HGF)0$$aNyquist, R. M.$$b3
000051337 7001_ $$0P:(DE-Juel1)VDB572$$aHeberle, J.$$b4$$uFZJ
000051337 773__ $$0PERI:(DE-600)1460391-3$$a10.1016/j.febslet.2006.01.055$$gVol. 580, p. 1350 - 1354$$p1350 - 1354$$q580<1350 - 1354$$tFEBS letters$$v580$$x0014-5793$$y2006
000051337 8567_ $$uhttp://dx.doi.org/10.1016/j.febslet.2006.01.055
000051337 909CO $$ooai:juser.fz-juelich.de:51337$$pVDB
000051337 9131_ $$0G:(DE-Juel1)FUEK409$$bGesundheit$$kP33$$lFunktion und Dysfunktion des Nervensystems$$vFunktion und Dysfunktion des Nervensystems$$x0
000051337 9141_ $$y2006
000051337 915__ $$0StatID:(DE-HGF)0010$$aJCR/ISI refereed
000051337 9201_ $$0I:(DE-Juel1)VDB58$$d31.12.2006$$gIBI$$kIBI-2$$lBiologische Strukturforschung$$x0
000051337 970__ $$aVDB:(DE-Juel1)80533
000051337 980__ $$aVDB
000051337 980__ $$aConvertedRecord
000051337 980__ $$ajournal
000051337 980__ $$aI:(DE-Juel1)ISB-2-20090406
000051337 980__ $$aUNRESTRICTED
000051337 980__ $$aI:(DE-Juel1)ICS-6-20110106
000051337 981__ $$aI:(DE-Juel1)IBI-7-20200312
000051337 981__ $$aI:(DE-Juel1)ISB-2-20090406
000051337 981__ $$aI:(DE-Juel1)ICS-6-20110106