TY  - JOUR
AU  - Pereira, M. M.
AU  - Sousa, F. L.
AU  - Teixeira, M.
AU  - Nyquist, R. M.
AU  - Heberle, J.
TI  - A tyrosine residue deprotonates during oxygen reduction by the caa3 reductase from Rhodothermus marinus
JO  - FEBS letters
VL  - 580
SN  - 0014-5793
CY  - Amsterdam [u.a.]
PB  - Elsevier
M1  - PreJuSER-51337
SP  - 1350 - 1354
PY  - 2006
N1  - Record converted from VDB: 12.11.2012
AB  - Heme-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.
KW  - Binding Sites
KW  - Catalysis
KW  - Cytochromes a3: metabolism
KW  - Oxidation-Reduction
KW  - Oxidoreductases
KW  - Oxygen: metabolism
KW  - Protons
KW  - Rhodobacter sphaeroides: enzymology
KW  - Rhodothermus: enzymology
KW  - Rhodothermus: metabolism
KW  - Spectroscopy, Fourier Transform Infrared
KW  - Tyrosine: chemistry
KW  - Cytochromes a3 (NLM Chemicals)
KW  - Protons (NLM Chemicals)
KW  - Tyrosine (NLM Chemicals)
KW  - Oxygen (NLM Chemicals)
KW  - Oxidoreductases (NLM Chemicals)
KW  - J (WoSType)
LB  - PUB:(DE-HGF)16
C6  - pmid:16466722
UR  - <Go to ISI:>//WOS:000235597700024
DO  - DOI:10.1016/j.febslet.2006.01.055
UR  - https://juser.fz-juelich.de/record/51337
ER  -