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Bacterial NADH-quinone oxidoreductases

Journal of Bioenergetics and Biomembranes, 1991
The NADH-quinone oxidoreductases of the bacterial respiratory chain could be divided in two groups depending on whether they bear an energy-coupling site. Those enzymes that bear the coupling site are designated as NADH dehydrogenase 1 (NDH-1) and those that do not as NADH dehydrogenase 2 (NDH-2).
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Pyridine Nucleotide — Disulfide Oxidoreductases

1980
Electron transfer between pyridine nucleotides and disulfide compounds is catalyzed by three flavoproteins which are well characterized. Lipoamide dehydrogenase reoxidizes reduced lipoamide (lip-(SH)2) by NAD+. Glutathione reductase catalyzes reduction of glutathione (GSSG) by NADPH. Thioredoxin reductase catalyzes the reduction of oxidized thioredoxin
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2031 oxidoreductase

2005
Method of identifying an anti-fungal agent which targets an essential protein or gene of a fungus comprising contacting a candidate substance with (i) a NADH:flavin oxidoreductase protein which comprises the sequence shown by SEQ ID N0:3, (ii) a NADH:flavin oxidoreductase protein which is a homologue of (i) and which comprises the sequence shown by SEQ
Lavens, S E   +4 more
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NADH-ubiquinone oxidoreductase

Biochimica et Biophysica Acta (BBA) - Reviews on Bioenergetics, 1976
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2031 oxidoreductase

Method of identifying an anti-fungal agent which targets an essential protein or gene of a fungus comprising contacting a candidate substance with (i) a NADH:flavin oxidoreductase protein which comprises the sequence shown by SEQ ID N0:3, (ii) a NADH:flavin oxidoreductase protein which is a homologue of (i) and which comprises the sequence shown by SEQ
openaire  

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