My watch list  

High potential iron-sulfur protein

High potential iron-sulfur protein
Symbol HIPIP
Pfam PF01355
InterPro IPR000170
SCOP 1hpi
OPM family 124
OPM protein 1hpi
Available PDB structures:

1hlqB:7-72 1hpi :6-69 1hrr :46-118 1ckuA:46-118 1neh :46-118 1js2A:46-118 1b0yA:46-118 1hrq :46-118 1noe :46-118 1hip :46-118 1eytA:9-79 1iuaA:9-79 3hipC:8-78 1pij :2-68 2hipB:2-68 1pih :2-68

High potential iron-sulphur proteins (HIPIP)[1] are a specific class of high-redox potential 4Fe-4S ferredoxins that functions in anaerobic electron transport and which occurs in photosynthetic bacteria and in Paracoccus denitrificans. 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-sulphur cluster is bound by four conserved cysteine residues.

                          [ 4Fe-4S cluster]
                          | |       |     |

'C': conserved cysteine involved in the binding of the iron-sulphur cluster.


  1. ^ Meyer TE, Breiter DR, Rayment I, Holden HM (1991). "The molecular structure of the high potential iron-sulfur protein isolated from Ectothiorhodospira halophila determined at 2.5-A resolution". J. Biol. Chem. 266 (28): 18660-18667. PMID 1917989.

Further reading

  • Crystal structures of photosynthetic reaction center and high-potential iron-sulfur protein from Thermochromatium tepidum, thermostability and electron transfer. Nogi T, Fathir I, Kobayashi M, Nozawa T, Miki K; Proc Natl Acad Sci U S A 2000;97:13561-13566. PubMed

This article includes text from the public domain Pfam and InterPro IPR000170

This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "High_potential_iron-sulfur_protein". A list of authors is available in Wikipedia.
Your browser is not current. Microsoft Internet Explorer 6.0 does not support some functions on Chemie.DE