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Mitic, S. (author), Strampraad, M.J.F. (author), Hagen, W.R. (author), de Vries, S. (author)
To afford mechanistic studies in enzyme kinetics and protein folding in the microsecond time domain we have developed a continuous-flow microsecond time-scale mixing instrument with an unprecedented dead-time of 3.8 ± 0.3 μs. The instrument employs a micro-mixer with a mixing time of 2.7 μs integrated with a 30 mm long flow-cell of 109 μm...
journal article 2017
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De Vries, S. (author), Dörner, K. (author), Strampraad, M.J.F. (author), Friedrich, T. (author)
Respiratory complex I converts the free energy of ubiquinone reduction by NADH into a proton motive force, a redox reaction catalyzed by flavin mononucleotide(FMN) and a chain of seven iron–sulfur centers. Electron transfer rates between the centers were determined by ultrafast freezequenching and analysis by EPR and UV/Vis spectroscopy. The...
journal article 2015
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De Vries, S. (author), Dörner, K. (author), Strampraad, M.J.F. (author), Friedrich, T. (author)
Der Atmungskettenkomplex I wandelt die freie Energie, die bei der Reduktion von Ubichinon durch NADH frei wird, in einen Protonengradienten über die Membran um. Die biologische Redoxreaktion wird von einem Flavinmononukleotid und einer Kette von sieben Eisen-Schwefel-Zentren katalysiert. Die Elektronentransfergeschwindigkeiten zwischen den...
journal article 2015
document
De Vries, S. (author), Dörner, K. (author), Strampraad, M.J.F. (author), Friedrich, T. (author)
Respiratory complex I converts the free energy of ubiquinone reduction by NADH into a proton motive force, a redox reaction catalyzed by flavin mononucleotide(FMN) and a chain of seven iron–sulfur centers. Electron transfer rates between the centers were determined by ultrafast freeze-quenching and analysis by EPR and UV/Vis spectroscopy. The...
journal article 2015
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