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SufS protein from Haloferax volcanii involved in Fe-S cluster assembly in haloarchaea

Basilio Zafrilla, Rosa María Martínez-Espinosa, Julia Esclapez, Francisco Pérez-Pomares, and María José Bonete

PROTEINS & PROTEOMICS 1804(7):7 (2010) PMID 20226884

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.

Copyright © 2010 Elsevier Ltd. All rights reserved.

DOI: 10.1016/j.bbapap.2010.03.001
Version: za2963e q8zad q8zb1 q8zc9 q8zdb q8zeb q8zfb q8zg7

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