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PubMed1992

Photothermal spectroscopy of bacteriochlorophyll-lipoprotein complexes.

Photoacoustic spectra at room and 85 K temperatures as well as photothermal beam deflection spectra of bacteriochlorophyll-lipoprotein complexes from purple bacterium Chromatium minutissimum were measured. Spectra were compared and obtained differences were tentatively explained by various inertion of these two methods. Photothermal beam deflection method measure the heat which is generated in close surroundings of absorbing pigment molecule, whereas usage of more inert photoacoustic signal is averaged over contributions from various pigments located in a larger sample volume and therefore is similar to absorption spectra.

Bacteriochlorophylls↗

PubMed1967

Thermodynamics of light emission and free-energy storage in photosynthesis.

A Planck law relationship between absorption and emission spectra is used to compute the fluorescence spectra of some photosynthetic systems from their absorption spectra. Calculated luminescence spectra of purple bacteria agree well but not perfectly with published experimental spectra. Application of the Planck law relation to published activation spectra for Systems I and II of spinach chloroplasts permits independent calculation of the luminescence spectra of the two systems; if the luminescence yield of System I is taken to be one-third the yield of System II, then the combined luminescence spectrum closely fits published experimental measurement.Consideration of the entropy associated with the excited state of the absorbing molecules is used to compute the oxidation-reduction potentials and maximum free-energy storage resulting from light absorption. Spinach chloroplasts under an illumination of 1 klux of white light can produce at most a potential difference of 1.32 ev for System I, and 1.36 ev for System II. In the absence of nonradiative losses, the maximum amount of free energy stored is 1.19 ev and 1.23 ev per photon absorbed for Systems I and II, respectively. The bacterium Chromatium under an illumination of 1 mw/cm(2) of Na D radiation can produce at most a potential difference of 0.90 ev; the maximum amount of free energy stored is 0.79 ev per photon absorbed.The combined effect of partial thermodynamic reversibility and a finite trapping rate on the amount of luminescence is considered briefly.

Chloroplasts↗

PubMed1991

Vibrational spectroscopy of excited electronic states in carotenoids in vivo. Picosecond time-resolved resonance Raman scattering.

The vibrational spectroscopy and population dynamics of excited singlet (2(1)Ag), excited triplet (3B u), and the ground (1Ag) electronic states of carotenoids in chromatophores of Chromatium vinosum (mainly spirilloxanthin and rhodopin) and of the same carotenoids in benzene solutions are examined by picosecond time-resolved resonance Raman scattering. Coherent Stokes Raman scattering from the ground states of carotenoids in chromatophores also is observed. Resonance Raman spectra of in vitro rhodopin and spirilloxanthin when compared with in vivo data demonstrate that scattering from spirilloxanthin dominates the in vivo spectrum. Comparisons of the time-dependent intensities of 2(1)Ag and 1Ag resonance Raman bands from both in vitro and in vivo carotenoids suggest that vibrationally excited levels in 1Ag are populated directly by the decay of the 2(1)Ag state and that these levels relax into a thermalized distribution in less than 50 ps. The appearance of asymmetrically broadened, ground-state resonance Raman bands supports this conclusion. Formation of the 3Bu state is observed for carotenoids in chromatophores, but not for in vitro spirilloxanthin indicating that the 3Bu state is formed by fission processes originating from the spatial organization of pigments within chromatophores. The rate at which the intensities of 2(1)Ag resonance Raman bands decay is faster for the carotenoids in vivo than for those in vitro thereby indicating that additional relaxation channels (e.g., energy transfer to bacteriochlorophylls) are present in the chromatophore. The similarity of the in vivo and in vitro 2(1)Ag resonance Raman spectra shows that no significant modifications in the vibronic coupling has been caused by the chromatophore environment.

Bacterial Chromatophores↗

PubMed2002

N-terminal methylation of the core light-harvesting complex in purple photosynthetic bacteria.

Several core light-harvesting complexes from both sulfur and non-sulfur purple photosynthetic bacteria have been identified to be methylated at the N-terminal alpha-amino group of beta-polypeptides by using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry and nuclear magnetic resonance. Monomethylation has been confirmed for the N-terminal alanine residues of the beta-polypeptides from Rhodospirillum rubrum, Thermochromatium tepidum and Chromatium vinosum, but not for the beta-polypeptide from Rhodobacter sphaeroides. The modification appears to be related with the amino acid sequence and charge distribution in the N-terminal end. Some common features and possible functions are discussed.

Chromatium↗

PubMed1991

Adduct formation between sulfite and the flavin of phototrophic bacterial flavocytochromes c. Kinetics of sequential bleach, recolor, and rebleach of flavin as a function of pH.

The kinetics of sulfite adduct formation with the bound flavin in flavocytochromes c from the purple phototrophic bacterium Chromatium vinosum and the green phototrophic bacterium Chlorobium thiosulfatophilum have been investigated as a function of pH. Both species of flavocytochrome c rapidly react with sulfite to form a flavin sulfite adduct (k = 10(3)-10(5) M-1 s-1) which is bleached at 450-475 nm and has associated charge-transfer absorbance at 660 nm. The rate constant for adduct formation in flavocytochrome c is 2-4 orders of magnitude faster than for model flavins of comparable redox potential and is likely to be due to a basic residue near the N-1 position of the flavin, which not only raises the redox potential but also stabilizes the negatively charged adduct. There is a pK for adduct formation at 6.5, which suggests that the order of magnitude larger rate constant at pH 5 as compared to pH 10 in flavocytochrome c is due the influence of another positive charge, possibly a protonated histidine residue. The adduct is indefinitely stable at pH 5 but decomposes (the flavin recolors) in a first-order process accelerating above pH 6 (at pH 10, k = 0.1 s-1). The pK for recoloring is 8.5, which is suggestive of a cysteine sulfhydryl. On the basis of the observed pK and available chemical information, we believe that recoloring is due to a secondary effect of the reaction of sulfite with a protein cystine disulfide, which is adjacent to the flavin.(ABSTRACT TRUNCATED AT 250 WORDS)

Bacteria↗

PubMed2001

Mechanistic studies on class I polyhydroxybutyrate (PHB) synthase from Ralstonia eutropha: class I and III synthases share a similar catalytic mechanism.

The Class I and III polyhydroxybutyrate (PHB) synthases from Ralstonia eutropha and Chromatium vinosum, respectively, catalyze the polymerization of beta-hydroxybutyryl-coenzyme A (HBCoA) to generate PHB. These synthases have different molecular weights, subunit composition, and kinetic properties. Recent studies with the C. vinosum synthase suggested that it is structurally homologous to bacterial lipases and allowed identification of active site residues important for catalysis [Jia, Y., Kappock, T. J., Frick, T., Sinskey, A. J., and Stubbe, J. (2000) Biochemistry 39, 3927-3936]. Sequence alignments between the Class I and III synthases revealed similar residues in the R. eutropha synthase. Site-directed mutants of these residues were prepared and examined using HBCoA and a terminally saturated trimer of HBCoA (sT-CoA) as probes. These studies reveal that the R. eutropha synthase possesses an essential catalytic dyad (C319-H508) in which the C319 is involved in covalent catalysis. A conserved Asp, D480, was shown not to be required for acylation of C319 by sT-CoA and is proposed to function as a general base catalyst to activate the hydroxyl of HBCoA for ester formation. Studies of the [(3)H]sT-CoA with wild-type and mutant synthases reveal that 0.5 equiv of radiolabel is covalently bound per monomer of synthase, suggesting that a dimeric form of the enzyme is involved in elongation. These studies, in conjunction with search algorithms for secondary structure, suggest that the Class I and III synthases are mechanistically similar and structurally homologous, despite their physical and kinetic differences.

Acyl Coenzyme A↗

PubMed1984

Cytochromes c' in their reaction with ethyl isocyanide.

The binding of ethyl isocyanide (EIC) to a representative number of cytochromes c' is demonstrated. Spectroscopic and equilibrium constants have been measured and compared for the binding of EIC to cytochromes c' from the photosynthetic bacteria Chromatium vinosum, Rhodopseudomonas palustris, Rhodospirillum rubrum, and Rhodopseudomonas sphaeroides. While the absorption spectra of the EIC complexes resemble those of EIC complexes of other high-spin hemoproteins, the Soret half band widths and extinction coefficients per heme exhibit more than a 2-fold difference with the values of C. vinosum being most similar to those of Rh. sphaeroides and of Rh. palustris similar to those of Rs. rubrum. The cytochromes exhibit binding equilibria consistent with the ligation of one molecule of EIC per heme in contrast to the reported binding of more than one molecule of CO per heme. The binding constants exhibit more than a 1000-fold difference with the values of C. vinosum being closely similar to those of Rh. sphaeroides and of Rh. palustris similar to those of Rs. rubrum. The lack of correlation between EIC and CO binding properties indicates that electronic factors do not determine the difference in EIC binding properties. The observed correlation between the extinction coefficients, half band widths, and equilibrium constants for EIC complex formation provides the first spectroscopic evidence that the differences in binding properties are associated with sterically hindered ligation to the heme. Although the differences in binding properties provide evidence of steric hindrance, the EIC binding constants for particular cytochromes c' indicate that the distal heme binding site is more accessible than previously indicated.(ABSTRACT TRUNCATED AT 250 WORDS)

Amino Acid Sequence↗

PubMed1985

Flavocytochromes c: transient kinetics of photoreduction by flavin analogues.

Kinetics of reduction of phototrophic bacterial flavocytochromes c by exogenous flavin semiquinones and fully reduced flavins generated by laser flash photolysis have been studied. The mechanisms of reduction of Chromatium and Chlorobium flavocytochromes c are more similar to one another than previously thought. Neither protein is very reactive with neutral flavin semiquinones (k less than 10(7) M-1 s-1), and the reactions with fully reduced flavins are slower than expected on the basis of comparison with other electron-transfer proteins of similar redox potentials. Deazaflavin radical is reactive with the flavocytochromes c by virtue of its low redox potential, but this reaction is also slower than expected on the basis of comparison with other electron-transfer proteins. These experiments indicate that the active site for reduction of flavocytochrome c is relatively buried and probably inaccessible to solvent. Fully reduced FMN does not show an ionic strength effect in its reaction with flavocytochrome c, which demonstrates that the active site is uncharged. Sulfite, which forms an adduct with protein-bound FAD, partially blocks heme reduction. This shows that heme is reduced via the FAD. The rate constant for intramolecular electron transfer between FAD and heme must be on the order of 10(4) s-1 or larger.

Bacteria↗

PubMed1985

Circular dichroism and redox properties of high redox potential ferredoxins.

The circular dichroism (CD) spectra of 13 examples of high-potential iron-sulfur proteins (HiPIPs), a class of [4Fe-4S] ferredoxins, have been determined. In contrast to the proposal of Carter [Carter, C. W., Jr. (1977) J. Biol. Chem. 252, 7802-7811], no strict correlation between visible CD features and utilization of the [4Fe-4S]2+/[4Fe-4S]3+ oxidation levels was found. Although most HiPIPs have these features, the model requires their presence in all species. There is also no simple relationship between CD spectral features and the presence of conserved tyrosine-19. In addition, no apparent correlation between CD properties and oxidation-reduction potential could be detected. However, amino acid side chains in close contact to the iron-sulfur cluster appear to be important in modulating spectral and oxidation-reduction properties. In particular, the negative shoulder at 290 nm and negative maximum at 230 nm correlate with the presence of Trp-80 (Chromatium vinosum numbering). Two HiPIPs that do not have Trp at this position have positive bands at 290 and 230 nm. These bands in the Ectothiorhodospira halophila HiPIPs are apparently associated with Trp-49, which is located on the opposite side of the effective mirror plane of the cluster from Trp-80. The effect of pH on circular dichroism and redox potential in Thiocapsa roseopersicina HiPIP, which has a histidine at position 49, is consistent with the interaction of the side chain with the cluster. Despite specific differences in their CD spectra, the various HiPIPs studied show general similarity consistent with structural homology within this class of iron-sulfur proteins.

Amino Acid Sequence↗

PubMed1981

High-potential iron-sulfur proteins and their possible site of electron transfer.

The electron-transfer mechanism of the Fe4S4 high-potential iron-sulfur proteins (HiPIP's) was explored via a stopped-flow spectrophotometric kinetic study of the reduction of Chromatium vinosum and Rhodopseudomonas gelatinosa HiPIP's by both native and trinitrophenyllysine-13 horse cytochrome c. The influence of electrostatic effects was also effectively partitioned from the redox process per se. The corrected rates were 12.3 X 10(4) and 3.8 X 10(4) M-1 s-1 for native with C. vinosum and R. gelatinosa HiPIP, respectively, and 17.5 X 10(4) and 5.46 X 10(4) M-1 s-1 for TNP-cytochrome c with the two HiPIP's, respectively. The faster rates of TNP-cytochrome c with the HiPIP's are unexpected in terms of possible steric interaction since lysine-13 is at the top of the heme crevice. In understanding the somewhat faster rates of the TNP-cytochrome c over native cytochrome c it is possible that (1) TNP-cytochrome c reacts more quickly since modification of the lysine-13 residue destabilizes somewhat the heme crevice or (2) in light of the hydrophobic nature of the trinitrophenyl group and the X-ray crystallographic structure of HiPIP, the TNP group facilitates electron transfer by interacting with a hydrophobic region on the HiPIP molecular surface. The region about the S4 sulfur atom is the most exposed and accessible hydrophobic region on the HiPIP surface, in addition to being the point of closest approach of the S4 to the external environment.

Animals↗

PubMed1980

Chromophore interactions in flavocytochrome c552: a resonance Raman investigation.

Resonance Raman spectra with both Soret and visible excitation have been obtained for Chromatium flavocytochrome c552 and its isolated diheme subunit under varying conditions of pH and inhibitor binding. The spectra are generally consistent with previously established classification schemes for porphyrin ring vibrations. The presence of covalently bound flavin in the protein was apparent in the fluorescent background it produced and in flavin-mediated photoeffects observed in heme Raman spectra obtained at high laser power. No flavin modes were present in the Raman spectra, nor was any evidence of direct heme-flavin interaction found by using this technique; however, a systematic perturbation of heme B1g vibrational frequencies was found in the oxidized holoprotein. The heme vibrational frequencies of c552 are compared to those of the diheme peptide and of other c-type cytochromes. They are consistent with an interpretation that involves pH-dependent changes in axial ligation and treats the hemes and flavin as isolated chromphores communicating via protein-mediated interactions.

Chromatium↗

PubMed1977

Near-infrared magnetic circular dichroism of cytochrome c'.

The near-infrared magnetic circular dichroism (MCD) of Rhodospirillum rubrum, Chromatium vinosum, and Rhodopseudomonas palustris cytochromes c' are reported. The spectra of the reduced protein are very similar to those of deoxymyoglobin. The spectra of the oxidized proteins in the pD range 1-13 can be analyzed on the basis of four species A, B, C, and D. The existence of nine species, reported in a recent electron paramagnetic resonance study, is not substantiated. The MCD spectra support the assignment of B as high spin and C and D as low spin. The MCD of species A is close to that of high-spin proteins and does not support the recently proposed assignment of a mixed high- and intermediate-spin ground state for this species. The energies of the near-IR electronic transitions of all four oxidized species point to axial ligation via oxygen, assuming histidine to be the opposite axial ligand. Unfortunately, insufficient model compounds with ligation by carboxyl or hydroxyl moieties exist to enable more precise assignments.

Chromatium↗

PubMed2002

Mechanism and biological role of nitric oxide binding to cytochrome c'.

The binding of nitric oxide to ferric and ferrous Chromatium vinosum cytochrome c' was studied. The extinction coefficients for the ferric and ferrous nitric oxide complexes were measured. A binding model that included both a conformational change and dissociation of the dimer into subunits provided the best fit for the ferric cytochrome c' data. The NO (nitric oxide) binding affinity of the WT ferric form was found to be comparable to the affinities displayed by the ferric myoglobins and hemoglobins. Using an improved fitting model, positive cooperativity was found for the binding of NO to the WT ferric and ferrous forms, while anticooperativity was the case for the Y16F mutant. Structural explanations accounting for the binding are proposed. The NO affinity of ferrous cytochrome c' was found to be much lower than the affinities of myoglobins, hemoglobins, and pentacoordinate heme models. Structural factors accounting for the difference in affinities were analyzed. The NO affinity of ferrous cytochrome c' was found to be in the range typical of receptors and carriers. In addition, cytochrome c' was found to react with cytosolic light-irradiated membranes in the presence of succinate and carbon monoxide. With these results, a biochemical model of cytochrome c' functioning as a nitric oxide carrier was proposed.

Amino Acid Substitution↗

PubMed1996

Use of 1H longitudinal relaxation times in the solution structure of paramagnetic proteins. Application to [4Fe-4S] proteins.

The accuracy of the solution structures determined by NMR is often poor around paramagnetic centers because the properties of the near protons are strongly perturbed by the electronic spin. The structural information contained in the relaxation rates of these protons has been extracted here by measuring the longitudinal relaxation times with the inversion-recovery total correlation spectroscopy (IR-TOCSY) sequence based on the recovery of cross peaks. In addition to measurements with nonselective inversion-recovery for nonoverlapping signals, reliable data have been obtained for a majority of main-chain protons from Chromatium vinosum high-potential ferredoxin. When a small and constant contribution from diamagnetism as well as the electronic spin distribution over the [4Fe-4S] cluster are taken into account, the shortest longitudinal relaxation times depend directly on the distance separating the protons from the paramagnetic center. This indicates that electron-nuclei dipolar interactions are the most efficient relaxation mechanism for these protons. However, the expected dependence of the relaxation rates as the sixth power of the distance has to be corrected because of induced relaxation among fast relaxing protons. This approach reveals that the solution structure of the protein is significantly different from the crystal structure around Phe-48. In addition, it provides an independent confirmation of the actual electronic structure of the [4Fe-4S]3+ cluster in the protein. The method devised in this work, which does not rely on specific enrichment, should be useful to improve the determination of NMR-derived solution structures of paramagnetic macromolecules.

Bacterial Proteins↗

PubMed1997

Characterization of a partially unfolded high potential iron protein.

A partially unfolded state of the Fe4S4-containing high potential iron-sulfur protein from Chromatium vinosum has been detected and characterized by NMR spectroscopy following addition of a concentrated solution of guanidinium chloride to the native protein. This intermediate species (i) maintains the polymetallic center, (ii) exhibits a largely collapsed secondary structure, and (iii) undergoes fast cluster decomposition upon oxidation. This information is framed into the knowledge about this class of proteins, and the possible role of this intermediate with respect to the in vivo folding/unfolding process is discussed as well its role in the slow hydrolytic degradation characteristic of oxidized HiPIPs.

Chromatium↗

PubMed2000

Unusual spectroscopic and electrochemical properties of the 2[4Fe-4S] ferredoxin of Thauera aromatica.

A reduced ferredoxin serves as the natural electron donor for key enzymes of the anaerobic aromatic metabolism in the denitrifying bacterium Thauera aromatica. It contains two [4Fe-4S] clusters and belongs to the Chromatium vinosum type of ferredoxins (CvFd) which differ from the "clostridial" type by a six-amino acid insertion between two successive cysteines and a C-terminal alpha-helical amino acid extension. The electrochemical and electron paramagnetic resonance (EPR) spectroscopic properties of both [4Fe-4S] clusters from T. aromatica ferredoxin have been investigated using cyclic voltammetry and multifrequency EPR. Results obtained from cyclic voltammetry revealed the presence of two redox transitions at -431 and -587 mV versus SHE. X-band EPR spectra recorded at potentials where only one cluster was reduced (greater than -500 mV) indicated the presence of a spin mixture of S = (3)/(2) and (5)/(2) spin states of one reduced [4Fe-4S] cluster. No typical S = (1)/(2) EPR signals were observed. At lower potentials (less than -500 mV), the more negative [4Fe-4S] cluster displayed Q-, X-, and S-band EPR spectra at 20 K which were typical of a single S = (1)/(2) low-spin [4Fe-4S] cluster with a g(av) of 1.94. However, when the temperature was decreased stepwise to 4 K, a magnetic interaction between the two clusters gradually became observable as a temperature-dependent splitting of both the S = (1)/(2) and S = (5)/(2) EPR signals. At potentials where both clusters were reduced, additional low-field EPR signals were observed which can only be assigned to spin states with spins of >(5)/(2). The results that were obtained establish that the common typical amino acid sequence features of CvFd-type ferredoxins determine the unusual electrochemical properties of the [4Fe-4S] clusters. The observation of different spin states in T. aromatica ferredoxin is novel among CvFd-type ferredoxins.

Amino Acid Sequence↗

PubMed1973

The amino acid sequence of cytochrome c' from Alcaligenes sp. N.C.I.B. 11015.

The amino acid sequence of the cytochrome c' from Alcaligenes sp. N.C.I.B. 11015 (Iwasaki's ;Pseudomonas denitrificans') has been determined. This organism is the only non-photosynthetic bacterium in which the protein has been found. The protein consists of a single polypeptide chain of 127 residues, with a single haem covalently attached to two cysteines. Unlike normal cytochromes c, the haem attachment site is very close to the C-terminus. The amino acid sequence around the haem attachment site is very similar to that of Chromatium vinosum D cytochrome c'. Detailed evidence for the amino acid sequence of the protein has been deposited as Supplementary Publication SUP 50022 at the British Library (Lending Division), (formerly the National Lending Library for Science and Technology), Boston Spa, Yorks. LS23 7BQ, U.K., from whom copies may be obtained on the terms given in Biochem. J. (1973) 131, 5.

Alcaligenes↗

PubMed1975

X-ray photoelectron spectra of iron-sulphur proteins.

The X-ray photoelectron spectra of the 2p, 3s and 3p levels of iron in oxidized Clostridium pasteurianum ferredoxin indicate that the eight iron atoms in the molecule are indistinguishable. Their magnetic state is indicated both by core polarization splitting of the 3s electrons, and by "shake-up' satellites on the 2p lines. Similar satellites are observed in the 2p lines of reduced Chromatium high-potential iron-sulphur proteins and oxidized spinach ferredoxin, indicating that there too the iron atoms are magnetic. The low observed magnetic susceptibility of these proteins is therefore due to spin-coupling between the iron atoms in the active centre.

Chromatium↗