1887

Abstract

Summary: Nitrate reductase from the yeast was found to contain one molecule of cytochrome and one atom of molybdenum per subunit. FAD/haem-dependent diaphorase activity (haem domain) was associated with a 40 kDa tryptic fragment of the subunit. The 50 amino-terminal residues of this fragment were determined, and the sequence did not show significant similarity to deduced sequences of other nitrate reductases previously published. Increasing ionic strength had a stimulatory effect on enzymic activity via stimulation of the molybdenum-dependent terminal nitrate-reducing activity. Stimulation of activity by exogenous protein (bovine serum albumin or casein) also appeared to be an ionic effect. Stimulation of catalytic activity by phosphate was a separate effect.

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/content/journal/micro/10.1099/00221287-139-3-473
1993-03-01
2020-10-24
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http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-139-3-473
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