A tyrosine residue deprotonates during oxygen reduction by the caa3 reductase from Rhodothermus marinus

Pereira MM, Sousa FL, Teixeira M, Nyquist RM, Heberle J (2006)
FEBS LETTERS 580(5): 1350-1354.

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Zeitschriftenaufsatz | Veröffentlicht | Englisch
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Abstract / Bemerkung
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 thermobalophilic Rhodothermus marinus becomes deprotonated in the transition from the oxidized state to the catalytic intermediate ferryl state Pm. 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. (c) 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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FEBS LETTERS
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580
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5
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1350-1354
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Pereira MM, Sousa FL, Teixeira M, Nyquist RM, Heberle J. A tyrosine residue deprotonates during oxygen reduction by the caa3 reductase from Rhodothermus marinus. FEBS LETTERS. 2006;580(5):1350-1354.
Pereira, M. M., Sousa, F. L., Teixeira, M., Nyquist, R. M., & Heberle, J. (2006). A tyrosine residue deprotonates during oxygen reduction by the caa3 reductase from Rhodothermus marinus. FEBS LETTERS, 580(5), 1350-1354. doi:10.1016/j.febslet.2006.01.055
Pereira, M. M., Sousa, F. L., Teixeira, M., Nyquist, R. M., and Heberle, J. (2006). A tyrosine residue deprotonates during oxygen reduction by the caa3 reductase from Rhodothermus marinus. FEBS LETTERS 580, 1350-1354.
Pereira, M.M., et al., 2006. A tyrosine residue deprotonates during oxygen reduction by the caa3 reductase from Rhodothermus marinus. FEBS LETTERS, 580(5), p 1350-1354.
M.M. Pereira, et al., “A tyrosine residue deprotonates during oxygen reduction by the caa3 reductase from Rhodothermus marinus”, FEBS LETTERS, vol. 580, 2006, pp. 1350-1354.
Pereira, M.M., Sousa, F.L., Teixeira, M., Nyquist, R.M., Heberle, J.: A tyrosine residue deprotonates during oxygen reduction by the caa3 reductase from Rhodothermus marinus. FEBS LETTERS. 580, 1350-1354 (2006).
Pereira, MM, Sousa, FL, Teixeira, M, Nyquist, RM, and Heberle, J. “A tyrosine residue deprotonates during oxygen reduction by the caa3 reductase from Rhodothermus marinus”. FEBS LETTERS 580.5 (2006): 1350-1354.

5 Zitationen in Europe PMC

Daten bereitgestellt von Europe PubMed Central.

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Molinas MF, Benavides L, Castro MA, Murgida DH., Bioelectrochemistry 105(), 2015
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Structural insights into electron transfer in caa3-type cytochrome oxidase.
Lyons JA, Aragão D, Slattery O, Pisliakov AV, Soulimane T, Caffrey M., Nature 487(7408), 2012
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Electron transfer dynamics of Rhodothermus marinus caa3 cytochrome c domains on biomimetic films.
Molinas MF, De Candia A, Szajnman SH, Rodríguez JB, Martí M, Pereira M, Teixeira M, Todorovic S, Murgida DH., Phys Chem Chem Phys 13(40), 2011
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The alternative complex III from Rhodothermus marinus - a prototype of a new family of quinol:electron acceptor oxidoreductases.
Pereira MM, Refojo PN, Hreggvidsson GO, Hjorleifsdottir S, Teixeira M., FEBS Lett 581(25), 2007
PMID: 17888426

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