Member database | Pfam |
Pfam type | family |
Short name | Prismane |
Author | Griffiths-Jones SR;0000-0001-6043-807X Bateman A;0000-0002-6982-4660 |
Sequence Ontology | 0100021 |
Description
This family includes both hybrid-cluster proteins and the beta chain of carbon monoxide dehydrogenase. The hybrid-cluster proteins contain two Fe/S centres - a [4Fe-4S] cubane cluster, and a hybrid [4Fe-2S-2O] cluster. The physiological role of this protein is as yet unknown, although a role in nitrate/nitrite respiration has been suggested
[2]. The prismane protein from Escherichia coli was shown to contain hydroxylamine reductase activity (NH2OH + 2e + 2 H+ -> NH3 + H2O). This activity is rather low. Hydroxylamine reductase activity was also found in CO-dehydrogenase in which the active site Ni was replaced by Fe
[1]. The CO dehydrogenase contains a Ni-3Fe-2S-3O centre.
References
1.Hydroxylamine reductase activity of the hybrid cluster protein from Escherichia coli. Wolfe MT, Heo J, Garavelli JS, Ludden PW. J. Bacteriol. 184, 5898-902, (2002). View articlePMID: 12374823
2.The hybrid-cluster protein ('prismane protein') from Escherichia coli. Characterization of the hybrid-cluster protein, redox properties of the [2Fe-2S] and [4Fe-2S-2O] clusters and identification of an associated NADH oxidoreductase containing FAD and [2Fe-2S]. van den Berg WA, Hagen WR, van Dongen WM. Eur. J. Biochem. 267, 666-76, (2000). View articlePMID: 10651802