Isolation, Characterization, and Functional Role of the High-Potential Iron-Sulfur Protein (HiPIP) from Rhodoferax fermentans

Hochkoeppler, Alejandro; Kofod, Pauli; Ferro, G.; Ciurli, Stefano

doi:10.1006/abbi.1995.1469

Cited by 27 publications

(28 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Taking this shift in redox potential into account, the initially proposed H1 potential yields a correct prediction of the observed electron transfer rates (see Table 2, which is published as supporting information on the PNAS web site). In the case of Rhodoferax fermentans, the redox potentials of the soluble HiPIP and H1 are ϩ351 mV and ϩ79 or 0 mV (the arrangements of the two low potential hemes has not yet been determined), respectively (45,46). The published value of t 1/2 ϭ 2.4 s value for electron transfer from HiPIP to the RC in this species can be rationalized only if either the redox potential of the complexed HIPIP is significantly lower than that of the soluble form or if the HiPIP binds significantly closer to H1 of the tetraheme subunit than in the other species mentioned above.…”

Section: Kinetics and Energetics Of The Donation Reaction From Hipip mentioning

confidence: 99%

Study of the high-potential iron sulfur protein in Halorhodospira halophila confirms that it is distinct from cytochrome c as electron carrier

Lieutaud

Alric

Bauzan

et al. 2005

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

The role of high-potential iron sulfur protein (HiPIP) in donating electrons to the photosynthetic reaction center in the halophilic ␥-proteobacterium Halorhodospira halophila was studied by EPR and time-resolved optical spectroscopy. A tight complex between HiPIP and the reaction center was observed. The EPR spectrum of HiPIP in this complex was drastically different from that of the purified protein and provides an analytical tool for the detection and characterization of the complexed form in samples ranging from whole cells to partially purified protein. The bound HiPIP was identified as iso-HiPIP II. Its Em value at pH 7 in the form bound to the reaction center was Ϸ100 mV higher (؉140 ؎ 20 mV) than that of the purified protein. EPR on oriented samples showed HiPIP II to be bound in a well defined geometry, indicating the presence of specific protein-protein interactions at the docking site. At moderately reducing conditions, the bound HiPIP II donates electrons to the cytochrome subunit bound to the reaction center with a half-time of <11 s. This donation reaction was analyzed by using Marcus's outer-sphere electron-transfer theory and compared with those observed in other HiPIP-containing purple bacteria. The results indicate substantial differences between the HiPIP-and the cytochrome c 2-mediated re-reduction of the reaction center.electron transfer ͉ photosynthesis ͉ electron paramagnetic resonance ͉ redox potential ͉ reaction center H igh-potential iron sulfur proteins (HiPIPs) are soluble electron carriers containing a single cubane [Fe 4 S 4 ] cluster [for reviews, see refs. 1 and 2] found in both photosynthetic (3-6) and nonphotosynthetic (7, 8) proteobacteria, as well as in members of the so-called FBC group (flexibacter, bacteroides, cytophaga group) (9). Despite three decades of detailed biophysical and biochemical characterization, the role of HiPIPs as physiological electron donors to the reaction center (RC) in photosynthesis and to oxidase in respiration was not demonstrated until 1995 (10-12).HiPIPs are commonly regarded as exotic substitutes for the ''normal'' soluble carrier cytochrome c. This notion is based on the presence of soluble cytochromes in mitochondrial respiration, in cyanobacterial photosynthesis, and in a variety of other prokaryotic energy conserving systems. Moreover, the usual ''workhorses'' in the study of purple bacterial photosynthesis, Rhodobacter sphaeroides, Rhodobacter capsulatus, and Blastochloris viridis, do not contain HiPIP. Instead, cytochrome c 2 , together with its various iso-forms, functions in their bioenergetic chains. Several decades of studies on these species have resulted in an understanding of the structural and functional details of electron donation from cytochrome c 2 to the photosynthetic RC (see, for example, refs. 13-19). In contrast, the interaction between HiPIP and RC is still poorly understood. Except for the case of Rubrivivax gelatinosus (20-23), only scarce data are available (24, 25). Surveys of photosynthetic electron transfer among p...

show abstract

Section: Kinetics and Energetics Of The Donation Reaction From Hipip mentioning

confidence: 99%

Study of the high-potential iron sulfur protein in Halorhodospira halophila confirms that it is distinct from cytochrome c as electron carrier

Lieutaud

Alric

Bauzan

et al. 2005

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

show abstract

“…On the basis of the high sequence similarity of Rf fermentans Hipip with the protein from Ru. gelatinosus, we are prompted to classify the former in the group of Hipips for which the cluster solvation, and not the overall charge, is important for determining the reduction potential (Em,, = +351 mV [7]). The presence of a single histidine residue in R$ fermentans Hipip can be utilized to check the validity of this proposal by measuring the pH dependence of the reduction potential.…”

Section: ---8 3 A3mentioning

confidence: 99%

“…It has been shown that the reduced Rf fermentans Hipip is an effective electron donor to the photosynthetic RC of the bacterium via the membrane-bound tetrahaem c-type cytochrome [7,12,131. Furthermore, the oxidized Hipip can be reduced by the bc, complex of Rf fermentans in a reaction inhibited by myxothiazol andor stigmatellin [20], which thus strongly suggests a role of this protein in the photosynthetic cycle.…”

Section: ---8 3 A3mentioning

confidence: 99%

“…Hipips are small-sized redox proteins that, in contrast to the low potential [4Fe-4S] ferredoxins, are characterized by reduction potentials in the range +50 to +450 mV [9, 101 and by [Fe4S413+''+ redox states [ll]. Experiments of light-induced oxidation of RC and membrane-bound c-type haem proteins have shown that RJ: fermentans Hipip is able to rapidly reduce the photo-oxidized photosynthetic RC through the reduction of the membranebound c-556 haem [7, 121. This process follows multiphasic kinetics, with a fast phase occumng within a HipiplRC complex [13].…”

mentioning

confidence: 99%

“…A high reduction potential soluble protein, present in light grown cells of RJ fermentans in larger amounts than the soluble cytochrome c, was shown to be an iron-sulfur protein (Hipip) by means of a variety of spectroscopic techniques [7,81. Hipips are small-sized redox proteins that, in contrast to the low potential [4Fe-4S] ferredoxins, are characterized by reduction potentials in the range +50 to +450 mV [9, 101 and by [Fe4S413+''+ redox states [ll].…”

mentioning

confidence: 99%

See 2 more Smart Citations

The Primary Structure of Rhodoferax fermentans High‐Potential Iron‐Sulfur Protein, an Electron Donor to the Photosynthetic Reaction Center

Driessche¹,

Ciurli

Hochkoeppler

et al. 1997

European Journal of Biochemistry

View full text Add to dashboard Cite

The complete amino acid sequence of Rhodoferax fermentans high-potential iron-sulfur protein (Hipip), which is known to be an efficient electron donor to the photosynthetic reaction center, has been determined using both N-terminal and C-terminal analyses. The sequence contains 75 residues, with 11 positive charges, 10 negative charges, and one histidine residue. The molecular mass of apo-Hipip, determined by electrospray ionization mass spectrometry, is 7849.64 Da. Multiple sequence alignment, based both on primary and tertiary structure information, reveals conservation of Tyrl9 and Gly75 ( Chromatium vinosum numbering) in addition to the four [Fe,S,]-bound cysteines. The Hipip from RJ fermentans is most similar (57 % similarity) to the Hipip from Rubrivivax gelatinosus, a photosynthetic bacterium belonging to the p-1 subgroup of the proteobacteria.Keywords: High-potential iron-sulfur protein ; Rhodoferax fermentans ; amino acid sequence ; mass spectrometry.Rhodoferax fermentans is a non-sulfur purple phototrophic bacterium belonging to the p group of phototrophic bacteria [ 1 -31. Sequence analyses of the 16s rDNA gene has shown that this bacterium is closely related to members of the chemotrophic family of the Comamonadaceae and less closely related to Rubrivivax gelatinosus (formerly called Rhodocyclus gelatinosus) [4], a non-sulfur purple bacterium, and to species of the genus Rhodocyclus.Light-grown cells of R$ fermentans contain one soluble ctype, four membrane-bound c-type, and three b-type haem proteins. Dark-grown cells, however, contain three membranebound c-type and four b-type haem proteins [5]. It has been shown that the membrane-bound c-type haem proteins from light-grown cells are able to reduce the photo-oxidized photosynthetic reaction center (RC) [6].A high reduction potential soluble protein, present in light grown cells of RJ fermentans in larger amounts than the soluble cytochrome c, was shown to be an iron-sulfur protein (Hipip) by means of a variety of spectroscopic techniques [7, 81. Hipips are small-sized redox proteins that, in contrast to the low potential [4Fe-4S] ferredoxins, are characterized by reduction potentials in the range +50 to +450 mV [9, 101 and by [Fe4S413+''+ redox states [ll]. Experiments of light-induced oxidation of RC and membrane-bound c-type haem proteins have shown that RJ: fermentans Hipip is able to rapidly reduce the photo-oxidized photosynthetic RC through the reduction of the membranebound c-556 haem [7, 121. This process follows multiphasic kinetics, with a fast phase occumng within a HipiplRC complex [13]. The high value of this electron transfer rate (t,,* = 2.2 ps) suggests a physiological role for Hipip in photocyclic electron transfer [13]. Recent evidence pointing to a physiological role for Hipips has also been established in Ru. gelatinosus whole cells [14]. Other functions, however, cannot be ruled out [ I 5 5 201. To deepen our understanding of the function of R& fermentans Hipip, to put the data obtained by NMR spectroscopy into focus [8], an...

show abstract

Coordination sphere versus protein environment as determinants of electronic and functional properties of iron-sulfur proteins

Capozzi

Ciurli

Luchinat

1998

Structure and Bonding

View full text Add to dashboard Cite

Isolation, Characterization, and Functional Role of the High-Potential Iron-Sulfur Protein (HiPIP) from Rhodoferax fermentans

Cited by 27 publications

References 0 publications

Study of the high-potential iron sulfur protein in Halorhodospira halophila confirms that it is distinct from cytochrome c as electron carrier

Study of the high-potential iron sulfur protein in Halorhodospira halophila confirms that it is distinct from cytochrome c as electron carrier

The Primary Structure of Rhodoferax fermentans High‐Potential Iron‐Sulfur Protein, an Electron Donor to the Photosynthetic Reaction Center

Coordination sphere versus protein environment as determinants of electronic and functional properties of iron-sulfur proteins

Contact Info

Product

Resources

About