Structural highlights
Function
HIP_RHOFE Specific class of high-redox-potential 4Fe-4S ferredoxins. Functions in anaerobic electron transport in most purple and in some other photosynthetic bacteria and in at least one genus (Paracoccus) of halophilic, denitrifying bacteria. Competent in photosynthetic electron transfer to oxidized cytochrome bc1 complex via the membrane-bound c-type tetraheme.[1] [:][2] [3] [4] [5]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
References
- ↑ Hochkoeppler A, Kofod P, Ferro G, Ciurli S. Isolation, characterization, and functional role of the high-potential iron-sulfur protein (HiPIP) from Rhodoferax fermentans. Arch Biochem Biophys. 1995 Oct 1;322(2):313-8. PMID:7574702 doi:http://dx.doi.org/10.1006/abbi.1995.1469
- ↑ Hochkoeppler A, Ciurli S, Venturoli G, Zannoni D. The high potential iron-sulfur protein (HiPIP) from Rhodoferax fermentans is competent in photosynthetic electron transfer. FEBS Lett. 1995 Jan 2;357(1):70-4. PMID:8001683
- ↑ Hochkoeppler A, Kofod P, Zannoni D. HiPiP oxido-reductase activity in membranes from aerobically grown cells of the facultative phototroph Rhodoferax fermentans. FEBS Lett. 1995 Nov 20;375(3):197-200. PMID:7498498
- ↑ Hochkoeppler A, Zannoni D, Ciurli S, Meyer TE, Cusanovich MA, Tollin G. Kinetics of photo-induced electron transfer from high-potential iron-sulfur protein to the photosynthetic reaction center of the purple phototroph Rhodoferax fermentans. Proc Natl Acad Sci U S A. 1996 Jul 9;93(14):6998-7002. PMID:8692932
- ↑ Bonora P, Principi I I, Monti B, Ciurli S, Zannoni D, Hochkoeppler A. On the role of high-potential iron-sulfur proteins and cytochromes in the respiratory chain of two facultative phototrophs Biochim Biophys Acta. 1999 Jan 27;1410(1):51-60. PMID:10076014
