Title : Purification and characterization of an NADH-hexacyanoferrate(III) reductase from spinach leaf plasma membrane.

Pub. Date : 1995 Jun 20

PMID : 7793986






2 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 The enzyme contained about one flavin adenine dinucleotide (FAD) per 45-kDa subunit as determined by fluorescence spectroscopy, was specific for the beta-hydrogen of NADH, preferred NADH over NADPH as electron donor, and preferred hexacyanoferrate(III) as electron acceptor, e.g., it reduced Fe3+-EDTA, cytochrome c, oxygen, and duroquinone at < 10% of the rate with hexacyanoferrate(III). NAD cytochrome c, somatic Homo sapiens
2 The enzyme contained about one flavin adenine dinucleotide (FAD) per 45-kDa subunit as determined by fluorescence spectroscopy, was specific for the beta-hydrogen of NADH, preferred NADH over NADPH as electron donor, and preferred hexacyanoferrate(III) as electron acceptor, e.g., it reduced Fe3+-EDTA, cytochrome c, oxygen, and duroquinone at < 10% of the rate with hexacyanoferrate(III). NAD cytochrome c, somatic Homo sapiens