@article{mbs:/content/journal/micro/10.1099/00221287-139-3-473, author = "Hipkin, Charles R. and Kau, David A. and Cannons, Andrew C.", title = "Further Characterization of the Assimilatory Nitrate Reductase from the Yeast Candida Nitratophila", journal= "Microbiology", year = "1993", volume = "139", number = "3", pages = "473-478", doi = "https://doi.org/10.1099/00221287-139-3-473", url = "https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-139-3-473", publisher = "Microbiology Society", issn = "1465-2080", type = "Journal Article", abstract = "Nitrate reductase from the yeast Candida nitratophila was found to contain one molecule of cytochrome b 557 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 in vitro 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.", }