NDLI: Hydroxylated naphthoquinones as substrates for Escherichia coli anaerobic reductases.

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Hydroxylated naphthoquinones as substrates for Escherichia coli anaerobic reductases.

Content Provider	Semantic Scholar
Author	Rothery, Richard A. Chatterjee, Indira Kiema, G. K. McDermott, Mark T. Weiner, Joel H.
Copyright Year	1998
Abstract	We have used two hydroxylated naphthoquinol menaquinol analogues, reduced plumbagin (PBH2, 5-hydroxy-2-methyl-1,4-naphthoquinol) and reduced lapachol [LPCH2, 2-hydroxy-3-(3-methyl-2-butenyl)-1, 4-naphthoquinol], as substrates for Escherichia coli anaerobic reductases. These compounds have optical, solubility and redox properties that make them suitable for use in studies of the enzymology of menaquinol oxidation. Oxidized plumbagin and oxidized lapachol have well resolved absorbances at 419 nm (epsilon=3.95 mM-1. cm-1) and 481 nm (epsilon=2.66 mM-1.cm-1) respectively (in Mops/KOH buffer, pH 7.0). PBH2 is a good substrate for nitrate reductase A (Km=282+/-28 microM, kcat=120+/-6 s-1) and fumarate reductase (Km=155+/-24 microM, kcat=30+/-2 s-1), but not for DMSO reductase. LPCH2 is a good substrate for nitrate reductase A (Km=57+/-35 microM, kcat=68+/-13 s-1), fumarate reductase (Km=85+/-27 microM, kcat=74+/-6 s-1) and DMSO reductase (Km=238+/-30 microM, kcat=191+/-21 s-1). The sensitivity of enzymic LPCH2 and PBH2 oxidation to 2-n-heptyl-4-hydroxyquinoline N-oxide inhibition is consistent with their oxidation occurring at sites of physiological quinol binding.
Starting Page	35
Ending Page	41
Page Count	7
File Format	PDF HTM / HTML
Alternate Webpage(s)	http://www.biochemj.org/content/ppbiochemj/332/1/35.full.pdf
PubMed reference number	9576848v1
Volume Number	332
Part	1
Journal	The Biochemical journal
Language	English
Access Restriction	Open
Subject Keyword	Buffers Dimethyl Sulfoxide Enzymatic Biochemistry Fumarates Naphthoquinones Nitrates Oxidoreductase Potassium Hydroxide Succinate Dehydrogenase hydroquinone binding lapachol nitrate reductase oxidation plumbagin
Content Type	Text
Resource Type	Article

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