High potential iron–sulfur proteins and their role as soluble electron carriers in bacterial photosynthesis: tale of a discovery
@article{Ciurli2004HighPI, title={High potential iron–sulfur proteins and their role as soluble electron carriers in bacterial photosynthesis: tale of a discovery}, author={Stefano Ciurli and Francesco Musiani}, journal={Photosynthesis Research}, year={2004}, volume={85}, pages={115-131} }
This review is an attempt to retrace the chronicle of the discovery of the role of high-potential iron–sulfur proteins (HiPIPs) as electron carriers in the photosynthetic chain of bacteria. Data and facts are presented through the magnifying lenses of the authors, using their best judgment to filter and elaborate on the many facets of the research carried out on this class of proteins over the years. The tale is divided into four main periods: the seeds, the blooming, the ripening, and the…
Figures and Tables from this paper
23 Citations
Crystal structure of a photosynthetic LH1-RC in complex with its electron donor HiPIP
- ChemistryNature communications
- 2021
Co-crystal structure of a bacterial photosynthetic electron transfer complex that employs weak hydrophobic interactions was achieved by using high-molar-ratio mixtures of a soluble donor protein with a membrane-embedded acceptor protein (reaction center, RC) at acidic pH.
The cytochrome c₈ involved in the nitrite reduction pathway acts also as electron donor to the photosynthetic reaction center in Rubrivivax gelatinosus.
- BiologyBiochimica et biophysica acta
- 2011
Metalloproteins Containing Cytochrome, Iron–Sulfur, or Copper Redox Centers
- ChemistryChemical reviews
- 2014
Through this review, structural features responsible for their redox properties are examined, including knowledge gained from recent progress in fine-tuning the redox centers.
Respiration and Respiratory Complexes
- Biology
- 2009
By modulating expression of different terminal oxido-reductases that lock onto a core electron transfer pathway, Rhodobacter species can survive in a range of oxic, micro-oxic, and anoxic environments either in the dark or in the light.
Iron–sulfur protein folds, iron–sulfur chemistry, and evolution
- BiologyJBIC Journal of Biological Inorganic Chemistry
- 2007
The data collected and analyzed here suggest that the extant structural landscape of Fe–S proteins has been shaped to a large extent by primeval geochemical conditions on one hand, and iron–sulfur chemistry on the other.
Functional Coupling Between Reaction Centers and Cytochrome bc 1 Complexes
- Biology
- 2009
In some Rhodobacter species, with a high bc 1:RC ratio, evidence has been found for the formation of specific supercomplexes associating all the components of the cyclic transfer in largely independent functional units.
Heterologous overproduction of 2[4Fe4S]- and [2Fe2S]-type clostridial ferredoxins and [2Fe2S]-type agrobacterial ferredoxin.
- BiologyProtein expression and purification
- 2016
From Genes to Metalloproteins: A Bioinformatic Approach
- Biology
- 2007
It was found that among the metals, zinc is required by the largest number of proteins in most organisms (on average, 10 % of the proteome in eukaryota is predicted to be zinc-binding), whereas copper is the least common.
References
SHOWING 1-10 OF 47 REFERENCES
The high potential iron‐sulfur protein (HiPIP) from Rhodoferax fermentans is competent in photosynthetic electron transfer
- Chemistry, BiologyFEBS letters
- 1995
Primary structure of a high potential iron sulfur protein from a moderately halophilic denitrifying coccus.
- BiologyThe Journal of biological chemistry
- 1977
High-potential iron-sulfur protein (HiPIP) is the major electron donor to the reaction center complex in photosynthetically growing cells of the purple bacterium Rubrivivax gelatinosus.
- BiologyBiochemistry
- 2002
It was concluded that HiPIP is the major physiological electron donor to the reaction center in Rvi.
Role of HiPIP as electron donor to the RC-bound cytochrome in photosynthetic purple bacteria
- BiologyPhotosynthesis Research
- 2004
High-Potential Iron-Sulfur Proteins play an important role in the reduction of the photo-oxidized RC-bound cytochrome in the following species: Ectothiorhodospira vacuolata, Chromatium vinosum, chromatium purpuratum and Rhodopila globiformis.
The distribution of soluble metallo-redox proteins in purple phototrophic bacteria.
- BiologyBiochimica et biophysica acta
- 1991
Chemical characterization of high potential iron proteins from Chromatium and Rhodopseudomonas gelatinosa.
- BiologyBiochimica et biophysica acta
- 1967
Interaction site for high-potential iron-sulfur protein on the tetraheme cytochrome subunit bound to the photosynthetic reaction center of Rubrivivax gelatinosus.
- Biology, ChemistryBiochemistry
- 1999
It is concluded that HiPIP, like soluble cytochromes, binds to the RC in the vicinity of the exposed part of the low-potential heme 1 of the cytochrome subunit, although some differences in the configurations of the hiPIP-RC and cy tochrome c-RC transient complexes may be postulated.
Isolation, characterization, and functional role of the high-potential iron-sulfur protein (HiPIP) from Rhodoferax fermentans.
- Chemistry, BiologyArchives of biochemistry and biophysics
- 1995
Kinetic studies of HiPIP oxidation, performed by monitoring the absorbance changes induced upon light excitation of the photosynthetic reaction center, give direct evidence of the role of the HiPIA in the photosynthesis electron transfer chain of Rf.
On the role of cytochrome c8 in photosynthetic electron transfer of the purple non-sulfur bacterium Rhodoferax fermentans
- Biology, ChemistryPhotosynthesis Research
- 2004
Competition experiments in the presence of both cytochrome c8 and high potential iron-sulfur protein (HiPIP), isolated from the same microorganism, show that cyto Chrome c8 oxidation is decreased upon addition of HiPIP, suggesting that cy tochrome c7 and HiPip might play alternative roles in the photosynthetic electron flow of Rhodoferax fermentans.
Amino Acid Sequences and Distribution of High-Potential Iron–Sulfur Proteins That Donate Electrons to the Photosynthetic Reaction Center in Phototropic Proteobacteria
- BiologyJournal of Molecular Evolution
- 2003
High-potential iron-sulfur protein (HiPIP) is likely to be the electron carrier of choice in the purple sulfur bacteria in the families Chromatiaceae and Ectothiorhodospiraceae, but the majority of purple nonsulfur bacteria are likely to utilize cytochrome c2.