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B6db references: 20226884

type Journal Article
authors Zafrilla B, Martínez-Espinosa RM, Esclapez J, Pérez-Pomares F, Bonete MJ.
title SufS protein from Haloferax volcanii involved in Fe-S cluster assembly in haloarchaea
journal Biochim Biophys Acta
sel selected
ui 20226884
year (2010)
volume 1804
pages 1476-82
abstract NifS-like proteins are pyridoxal 5'-phosphate (PLP)-dependent enzymes involved in sulphur transfer metabolism. These enzymes have been catalogued as cysteine desulphurases (CDs) which catalyse the conversion of L-cysteine into L-alanine and an enzyme-bound persulphide radical. This reaction, assisted by different scaffold protein machineries, seems to be the main source of sulphur for the synthesis of essential cofactors of the[Fe-S] cluster. CDs genes have been detected in the tree domains of life, but, up until now, there has been no biochemical characterisation or study into the physiological role of this enzyme in haloarchaea. In this study, we have cloned, expressed and characterised a cysteine desulphurase (SufS) from Haloferax volcanii and demonstrated that this protein is able to reconstitute the [Fe-S] cluster of halophilic ferredoxin.
last changed 2010/06/16 17:32

B6db references