Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Sarah R O'Kane"'
Publikováno v:
PLoS ONE, Vol 8, Iss 1, p e53559 (2013)
The Thermus thermophilus succinate:quinone reductase (SQR), serving as the respiratory complex II, has been homologously produced under the control of a constitutive promoter and subsequently purified. The detailed biochemical characterization of the
Externí odkaz:
https://doaj.org/article/d08d0cdf18834420bfe1182c5aa319ed
Autor:
Wolfgang Nitschke, Tewfik Soulimane, Christophe Léger, Olga Kolaj-Robin, Frauke Baymann, Sarah R. O'Kane
Publikováno v:
Biochimica et Biophysica Acta (BBA)-Reviews on Bioenergetics
Biochimica et Biophysica Acta (BBA)-Reviews on Bioenergetics, 2011, 1 (1807), pp.68-79
Biochimica et Biophysica Acta (BBA)-Reviews on Bioenergetics, Elsevier, 2011, 1 (1807), pp.68-79
Biochimica et Biophysica Acta (BBA)-Reviews on Bioenergetics, 2011, 1 (1807), pp.68-79
Biochimica et Biophysica Acta (BBA)-Reviews on Bioenergetics, Elsevier, 2011, 1 (1807), pp.68-79
Enzymes serving as respiratory complex II belong to the succinate:quinone oxidoreductases superfamily that comprises succinate:quinone reductases (SQRs) and quinol:fumarate reductases. The SQR from the extreme thermophile Thermus thermophilus has bee
Publikováno v:
Acta crystallographica. Section F, Structural biology and crystallization communications. 66(Pt 3)
The oxygenase HpaB is a component of the 4-hydroxyphenylacetate 3-monooxygenase enzyme that is responsible for the hydroxylation of 4-hydroxyphenylacetate. It utilizes molecular oxygen and a reduced flavin, which is provided by HpaC, the second com
Purification and characterisation of native and recombinant complex II from Thermus thermophilus HB8
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1797:17-18
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1817:S158
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1777:S95