• Prosthetic group features
• HiPIPs in motif databases
• HiPIPs in alignment databases
• HiPIPs in 3­D databases
• References

Iron-sulphur cluster	Formal oxidation states
[Fe4S4](SCys)4	[Fe4S4]2+; [Fe4S4]3+

High potential iron-sulphur proteins (HiPIPs) form a unique family of Fe₄S₄ ferredoxins that function in anaerobic electron transport chains; some have a redox potential higher than any other known iron-sulphur protein (e.g., HiPIP from Rhodopila globiformis has a redox potential of ca. 450 mV [1]). Several HiPIPs have so far been characterised structurally [2-5], their folds belonging to the +ß class. As in other bacterial ferredoxins, the [Fe₄S₄] cluster adopts a cubane­like conformation and is ligated to the protein via four cysteinyl sulphur ligands [2] (Figure 1ISU), which are located in type I turns [3].

HiPIPs in motif databases

PRINTS ID	PRINTS AC	PROSITE/BLOCKS ID	PROSITE AC	BLOCKS AC
HIPIPFRDOXIN	PR00374	HIPIP	PS00596	BL00596

HiPIPs in alignment databases

Protein Superfamily	Pfam	LPFC 3­D alignment
00032; high potential iron-sulfur protein	-	hip

PDB	scop	BSM	RELI Base	Header	¹
1b0y	-	1b0y	-	High­potential iron-sulphur protein H42Q mutant); Chromatium vinosum, strain XL1 Blue (recombinant form expressed in Escherichia coli	-
1hip	1hip	1hip	1hip	High­potential iron-sulphur protein (oxidised); Chromatium vinosum, strain D	-
1hpi	1hpi	1hpi	1hpi	High­potential iron-sulphur protein (oxidised); Ectothiorhodospira vacuolata	MS5MM5
1hrq	1hrq	1hrq	1hrq	High­potential iron-sulphur protein (reduced); Chromatium vinosum	-
1hrr	1hrr	1hrr	1hrr	High­potential iron-sulphur protein (reduced); Chromatium vinosum	-
1isu	1isu	1isu	1isu	High­potential iron-sulphur protein; Rhodocyclus tenuis	MMS93100
1neh	1neh	1neh	1neh	High­potential iron-sulphur protein (oxidised); Chromatium vinosum	-
1noe	1noe	1noe	1noe	High­potential iron-sulphur protein (reduced); Chromatium vinosum	-
1pih	1pih	1pih	1pih	High­potential iron-sulphur protein (insertion A1, S2 mutant); Ectothiorhodospira halophila (recombinant form expressed in Escherichia coli	MS5IB11
1pij	1pij	1pij	1pij	High­potential iron-sulphur protein (insertion A1, S2 mutant); Ectothiorhodospira halophila (recombinant form expressed in Escherichia coli	MS5IB11
2hip	2hip	2hip	2hip	High­potential iron-sulphur protein; Ectothiorhodospira halophila	MMS92088

¹ Macromolecular Structures abstract. Full text is available to BioMedNet Members

References

1. Ambler, R.P., Meyer, T.E. and Kamen, M.D.. (1993) Amino acid sequence of a high redox potential ferredoxin (HiPIP) from the purple phototrophic bacterium Rhodopila globiformis, which has the highest known redox potential of its class. Arch. Biochem. Biophys. 306, 215-222.
2. Breiter, D.R., Meyer, T.E., Rayment, I. and Holden, H.M. (1991) The molecular structure of the high potential iron-sulfur protein isolated from Ectothiorhodospira halophila determined at 2.5­Å resolution. J. Biol. Chem. 266, 18660-18667.
3. Rayment, I., Wesenberg, G., Meyer, T.E., Cusanovich, M.A. and Holden, H.M. (1992) Three­dimensional structure of the high­potential iron-sulfur protein isolated from the purple phototrophic bacterium Rhodocyclus tenuis determined and refined at 1.5 Å resolution. J. Mol. Biol. 228, 672-686.
4. Benning, M.M., Meyer, T.E., Rayment, I. and Holden, H.M. (1994) Molecular structure of the oxidized high­potential iron-sulfur protein isolated from Ectothiorhodospira vacuolata. Biochemistry 33, 2476-2483.
5. Banci, L., Bertini, I., Dikiy, A., Kastrau, D.H.W., Luchinat, C. and Sompornpisut, P. (1995) The three­dimensional solution structure of the reduced high­potential iron-sulfur protein from Chromatium vinosum through NMR. Biochemistry 34, 206-219.

Bibliography on structural studies of HiPIPs