PROSITE documentation PDOC00515
High potential iron-sulfur proteins family profile


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 [3]. 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          ]
                                      |  |             |             |
'C': conserved cysteine involved in the binding of the iron-sulfur cluster.
Last update:

April 2008 / Pattern removed, profile added and text revised.


Technical section

PROSITE method (with tools and information) covered by this documentation:

HIPIP, PS51373; High potential iron-sulfur proteins family profile  (MATRIX)


1AuthorsBreiter D.R. Meyer T.E. Rayment I. Holden H.M.
TitleThe molecular structure of the high potential iron-sulfur protein isolated from Ectothiorhodospira halophila determined at 2.5-A resolution.
SourceJ. Biol. Chem. 266:18660-18667(1991).
PubMed ID1917989

2AuthorsKusano T. Takeshima T. Sugawara K. Inoue C. Shiratori T. Yano T. Fukumori Y. Yamanaka T.
TitleMolecular cloning of the gene encoding Thiobacillus ferrooxidans Fe(II) oxidase. High homology of the gene product with HiPIP.
SourceJ. Biol. Chem. 267:11242-11247(1992).
PubMed ID1317860

3AuthorsVan 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.
TitleAmino acid sequences and distribution of high-potential iron-sulfur proteins that donate electrons to the photosynthetic reaction center in phototropic proteobacteria.
SourceJ. Mol. Evol. 57:181-199(2003).
PubMed ID14562962

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