|PROSITE documentation PDOC00515|
High potential iron-sulfur proteins (HiPIP) [1,2] are a specific class of high-redox potential 4Fe-4S ferredoxins that functions in anaerobic electron transport and which occurs commonly in purple photosynthetic bacteria and in other bacteria, such as Paracoccus denitrificans and Thiobacillus ferrooxidans . HiPIPs seem to react by oxidation of [4Fe-4S]2+ to [4Fe-4S]3+.
The HiPIPs are small proteins which show significant variation in their sequences, their sizes (from 63 to 85 amino acids), and in their oxidation-reduction potentials . As shown in the following schematic representation the iron-sulfur cluster is bound by four conserved cysteine residues.
[ 4Fe-4S cluster ] | | | | xxxxxxxxxxxxxxxxxxxxxxxxxxxxxxxxxxxxCxxCxxxxxxxxxxxxxCxxxxxxxxxxxxxCxxxxxxx
'C': conserved cysteine involved in the binding of the iron-sulfur cluster.Last update:
April 2008 / Pattern removed, profile added and text revised.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Breiter D.R. Meyer T.E. Rayment I. Holden H.M.|
|Title||The molecular structure of the high potential iron-sulfur protein isolated from Ectothiorhodospira halophila determined at 2.5-A resolution.|
|Source||J. Biol. Chem. 266:18660-18667(1991).|
|2||Authors||Kusano T. Takeshima T. Sugawara K. Inoue C. Shiratori T. Yano T. Fukumori Y. Yamanaka T.|
|Title||Molecular cloning of the gene encoding Thiobacillus ferrooxidans Fe(II) oxidase. High homology of the gene product with HiPIP.|
|Source||J. Biol. Chem. 267:11242-11247(1992).|
|3||Authors||Van Driessche G. Vandenberghe I. Devreese B. Samyn B. Meyer T.E. Leigh R. Cusanovich M.A. Bartsch R.G. Fischer U. Van Beeumen J.J.|
|Title||Amino acid sequences and distribution of high-potential iron-sulfur proteins that donate electrons to the photosynthetic reaction center in phototropic proteobacteria.|
|Source||J. Mol. Evol. 57:181-199(2003).|