High potential iron-sulfur protein

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]
                          | |       |     |
       xxxxxxxxxxxxxxxxxxxCxCxxxxxxxCxxxxxCxxxx

Additional recommended knowledge

How to ensure accurate weighing results every day?

Essential Laboratory Skills Guide

Daily Sensitivity Test

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

References

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