The Experts below are selected from a list of 180 Experts worldwide ranked by ideXlab platform
Michael A Cusanovich - One of the best experts on this subject based on the ideXlab platform.
-
identification of 42 possible cytochrome c genes in the shewanella oneidensis genome and characterization of six soluble Cytochromes
Omics A Journal of Integrative Biology, 2004Co-Authors: T E Meyer, A I Tsapin, Isabel Vandenberghe, Kenneth H Nealson, Michael A Cusanovich, Lina De Smet, Dmitrij Frishman, Jozef Van BeeumenAbstract:Through pattern matching of the cytochrome c heme-binding site (CXXCH) against the genome sequence of Shewanella oneidensis MR-1, we identified 42 possible cytochrome c genes (27 of which should be soluble) out of a total of 4758. However, we found only six soluble Cytochromes c in extracts of S. oneidensis grown under several different conditions: (1) a small tetraheme cytochrome c, (2) a tetraheme flavocytochrome c-fumarate reductase, (3) a diheme cytochrome c4, (4) a monoheme cytochrome c5, (5) a monoheme cytochrome c′, and (6) a diheme bacterial cytochrome c peroxidase. These Cytochromes were identified either through N-terminal or complete amino acid sequence determination combined with mass spectroscopy. All six Cytochromes were about 10-fold more abundant when cells were grown at low than at high aeration, whereas the flavocytochrome c-fumarate reductase was specifically induced by anaerobic growth on fumarate. When adjusted for the different heme content, the monoheme cytochrome c5 is as abundant ...
-
identification of 42 possible cytochrome c genes in the shewanella oneidensis genome and characterization of six soluble Cytochromes
Omics A Journal of Integrative Biology, 2004Co-Authors: T E Meyer, A I Tsapin, Isabel Vandenberghe, Kenneth H Nealson, Michael A Cusanovich, Lina De Smet, Dmitrij Frishman, J. Van BeeumenAbstract:Through pattern matching of the cytochrome c heme-binding site (CXXCH) against the genome sequence of Shewanella oneidensis MR-1, we identified 42 possible cytochrome c genes (27 of which should be soluble) out of a total of 4758. However, we found only six soluble Cytochromes c in extracts of S. oneidensis grown under several different conditions: (1) a small tetraheme cytochrome c, (2) a tetraheme flavocytochrome c-fumarate reductase, (3) a diheme cytochrome c4, (4) a monoheme cytochrome c5, (5) a monoheme cytochrome c', and (6) a diheme bacterial cytochrome c peroxidase. These Cytochromes were identified either through N-terminal or complete amino acid sequence determination combined with mass spectroscopy. All six Cytochromes were about 10-fold more abundant when cells were grown at low than at high aeration, whereas the flavocytochrome c-fumarate reductase was specifically induced by anaerobic growth on fumarate. When adjusted for the different heme content, the monoheme cytochrome c5 is as abundant as are the small tetraheme cytochrome and the tetraheme fumarate reductase. Published results on regulation of Cytochromes from DNA microarrays and 2D-PAGE differ somewhat from our results, emphasizing the importance of multifaceted analyses in proteomics.
-
Discovery and characterization of electron transfer proteins in the photosynthetic bacteria.
Photosynthesis research, 2003Co-Authors: Terrance E. Meyer, Michael A CusanovichAbstract:Research on photosynthetic electron transfer closely parallels that of other electron transfer pathways and in many cases they overlap. Thus, the first bacterial cytochrome to be characterized, called cytochrome c (2), is commonly found in non-sulfur purple photosynthetic bacteria and is a close homolog of mitochondrial cytochrome c. The cytochrome bc (1) complex is an integral part of photosynthetic electron transfer yet, like cytochrome c (2), was first recognized as a respiratory component. Cytochromes c (2) mediate electron transfer between the cytochrome bc (1) complex and photosynthetic reaction centers and cytochrome a-type oxidases. Not all photosynthetic bacteria contain cytochrome c (2); instead it is thought that HiPIP, auracyanin, Halorhodospira cytochrome c551, Chlorobium cytochrome c555, and cytochrome c (8) may function in a similar manner as photosynthetic electron carriers between the cytochrome bc (1) complex and reaction centers. More often than not, the soluble or periplasmic mediators do not interact directly with the reaction center bacteriochlorophyll, but require the presence of membrane-bound intermediates: a tetraheme cytochrome c in purple bacteria and a monoheme cytochrome c in green bacteria. Cyclic electron transfer in photosynthesis requires that the redox potential of the system be delicately poised for optimum efficiency. In fact, lack of redox poise may be one of the defects in the aerobic phototrophic bacteria. Thus, large concentrations of Cytochromes c (2) and c' may additionally poise the redox potential of the cyclic photosystem of purple bacteria. Other Cytochromes, such as flavocytochrome c (FCSD or SoxEF) and cytochrome c551 (SoxA), may feed electrons from sulfide, sulfur, and thiosulfate into the photosynthetic pathways via the same soluble carriers as are part of the cyclic system.
-
identification of a small tetraheme cytochrome c and a flavocytochrome c as two of the principal soluble Cytochromes c in shewanella oneidensis strain mr1
Applied and Environmental Microbiology, 2001Co-Authors: A I Tsapin, Isabel Vandenberghe, Kenneth H Nealson, J H Scott, T E Meyer, Michael A Cusanovich, E Harada, T Kaizu, Hideo Akutsu, David LeysAbstract:Two abundant, low-redox-potential Cytochromes c were purified from the facultative anaerobe Shewanella oneidensis strain MR1 grown anaerobically with fumarate. The small cytochrome was completely sequenced, and the genes coding for both proteins were cloned and sequenced. The small cytochrome c contains 91 residues and four heme binding sites. It is most similar to the Cytochromes c from Shewanella frigidimarina (formerly Shewanella putrefaciens) NCIMB400 and the unclassified bacterial strain H1R (64 and 55% identity, respectively). The amount of the small tetraheme cytochrome is regulated by anaerobiosis, but not by fumarate. The larger of the two low-potential Cytochromes contains tetraheme and flavin domains and is regulated by anaerobiosis and by fumarate and thus most nearly corresponds to the flavocytochrome c-fumarate reductase previously characterized from S. frigidimarina to which it is 59% identical. However, the genetic context of the cytochrome genes is not the same for the two Shewanella species, and they are not located in multicistronic operons. The small cytochrome c and the cytochrome domain of the flavocytochrome c are also homologous, showing 34% identity. Structural comparison shows that the Shewanella tetraheme Cytochromes are not related to the Desulfovibrio Cytochromes c3 but define a new folding motif for small multiheme Cytochromes c.
-
Structure and Characterization of Ectothiorhodospira vacuolata Cytochrome b 558, a Prokaryotic Homologue of Cytochrome b 5
The Journal of biological chemistry, 1999Co-Authors: Vesna Kostanjevecki, G. Van Driessche, Terrance E. Meyer, Michael A Cusanovich, D. Leys, Ulrich Fischer, Yves Guisez, J. Van BeeumenAbstract:Abstract A soluble cytochrome b 558from the purple phototropic bacterium Ectothiorhodospira vacuolata was completely sequenced by a combination of automated Edman degradation and mass spectrometry. The protein, with a measured mass of 10,094.7 Da, contains 90 residues and binds a single protoheme. Unexpectedly, the sequence shows homology to eukaryotic Cytochromesb 5. As no prokaryotic homologue had been reported so far, we developed a protocol for the expression, purification, and crystallization of recombinant cytochromeb 558. The structure was solved by molecular replacement to a resolution of 1.65 A. It shows that cytochromeb 558 is indeed the first bacterial cytochromeb 5 to be characterized and differs from its eukaryotic counterparts by the presence of a disulfide bridge and a four-residue insertion in front of the sixth ligand (histidine). Eukaryotes contain a variety of b 5 homologues, including soluble and membrane-bound multifunctional proteins as well as multidomain enzymes such as sulfite oxidase, fatty-acid desaturase, nitrate reductase, and lactate dehydrogenase. A search of theMycobacterium tuberculosis genome showed that a previously unidentified gene encodes a fatty-acid desaturase with an N-terminalb 5 domain. Thus, it may provide another example of a bacterial b 5 homologue.
T E Meyer - One of the best experts on this subject based on the ideXlab platform.
-
identification of 42 possible cytochrome c genes in the shewanella oneidensis genome and characterization of six soluble Cytochromes
Omics A Journal of Integrative Biology, 2004Co-Authors: T E Meyer, A I Tsapin, Isabel Vandenberghe, Kenneth H Nealson, Michael A Cusanovich, Lina De Smet, Dmitrij Frishman, Jozef Van BeeumenAbstract:Through pattern matching of the cytochrome c heme-binding site (CXXCH) against the genome sequence of Shewanella oneidensis MR-1, we identified 42 possible cytochrome c genes (27 of which should be soluble) out of a total of 4758. However, we found only six soluble Cytochromes c in extracts of S. oneidensis grown under several different conditions: (1) a small tetraheme cytochrome c, (2) a tetraheme flavocytochrome c-fumarate reductase, (3) a diheme cytochrome c4, (4) a monoheme cytochrome c5, (5) a monoheme cytochrome c′, and (6) a diheme bacterial cytochrome c peroxidase. These Cytochromes were identified either through N-terminal or complete amino acid sequence determination combined with mass spectroscopy. All six Cytochromes were about 10-fold more abundant when cells were grown at low than at high aeration, whereas the flavocytochrome c-fumarate reductase was specifically induced by anaerobic growth on fumarate. When adjusted for the different heme content, the monoheme cytochrome c5 is as abundant ...
-
identification of 42 possible cytochrome c genes in the shewanella oneidensis genome and characterization of six soluble Cytochromes
Omics A Journal of Integrative Biology, 2004Co-Authors: T E Meyer, A I Tsapin, Isabel Vandenberghe, Kenneth H Nealson, Michael A Cusanovich, Lina De Smet, Dmitrij Frishman, J. Van BeeumenAbstract:Through pattern matching of the cytochrome c heme-binding site (CXXCH) against the genome sequence of Shewanella oneidensis MR-1, we identified 42 possible cytochrome c genes (27 of which should be soluble) out of a total of 4758. However, we found only six soluble Cytochromes c in extracts of S. oneidensis grown under several different conditions: (1) a small tetraheme cytochrome c, (2) a tetraheme flavocytochrome c-fumarate reductase, (3) a diheme cytochrome c4, (4) a monoheme cytochrome c5, (5) a monoheme cytochrome c', and (6) a diheme bacterial cytochrome c peroxidase. These Cytochromes were identified either through N-terminal or complete amino acid sequence determination combined with mass spectroscopy. All six Cytochromes were about 10-fold more abundant when cells were grown at low than at high aeration, whereas the flavocytochrome c-fumarate reductase was specifically induced by anaerobic growth on fumarate. When adjusted for the different heme content, the monoheme cytochrome c5 is as abundant as are the small tetraheme cytochrome and the tetraheme fumarate reductase. Published results on regulation of Cytochromes from DNA microarrays and 2D-PAGE differ somewhat from our results, emphasizing the importance of multifaceted analyses in proteomics.
-
identification of a small tetraheme cytochrome c and a flavocytochrome c as two of the principal soluble Cytochromes c in shewanella oneidensis strain mr1
Applied and Environmental Microbiology, 2001Co-Authors: A I Tsapin, Isabel Vandenberghe, Kenneth H Nealson, J H Scott, T E Meyer, Michael A Cusanovich, E Harada, T Kaizu, Hideo Akutsu, David LeysAbstract:Two abundant, low-redox-potential Cytochromes c were purified from the facultative anaerobe Shewanella oneidensis strain MR1 grown anaerobically with fumarate. The small cytochrome was completely sequenced, and the genes coding for both proteins were cloned and sequenced. The small cytochrome c contains 91 residues and four heme binding sites. It is most similar to the Cytochromes c from Shewanella frigidimarina (formerly Shewanella putrefaciens) NCIMB400 and the unclassified bacterial strain H1R (64 and 55% identity, respectively). The amount of the small tetraheme cytochrome is regulated by anaerobiosis, but not by fumarate. The larger of the two low-potential Cytochromes contains tetraheme and flavin domains and is regulated by anaerobiosis and by fumarate and thus most nearly corresponds to the flavocytochrome c-fumarate reductase previously characterized from S. frigidimarina to which it is 59% identical. However, the genetic context of the cytochrome genes is not the same for the two Shewanella species, and they are not located in multicistronic operons. The small cytochrome c and the cytochrome domain of the flavocytochrome c are also homologous, showing 34% identity. Structural comparison shows that the Shewanella tetraheme Cytochromes are not related to the Desulfovibrio Cytochromes c3 but define a new folding motif for small multiheme Cytochromes c.
-
Electron transfer proteins of the purple phototrophic bacterium, Rhodopseudomonas rutila.
Archives of Biochemistry and Biophysics, 1991Co-Authors: R. G. Bartsch, U. Fischer, G. Van Driessche, J. Van Beeumen, J. Fitch, T E Meyer, Michael A CusanovichAbstract:Abstract The soluble electron transfer protein content of Rhodopseudomonas rutila was found to consist of two basic Cytochromes and a (4Fe-4S) ferredoxin. Cytochrome c ′ was easily identified by its characteristic high spin absorption spectra. The native molecular weight is 29,000 and the subunit is 14,000. Cytochrome c -550 has low spin absorption spectra and a high redox potential (376 mV) typical of Cytochromes c 2 . The molecular weight is about 14,000. The ferredoxin is apparently a dimer (43,000) of approximately 18,000 Da subunits. There are 1.3 to 1.5 iron-sulfur clusters per monomer of 18-to 21-kDa protein. The N-terminal amino acid sequence is like the (7Fe-8S) ferredoxins of Rhodobacter capsulatus and Azotobacter vinelandii . Remarkably, there are only 2 or 3 out of 25 amino acid substitutions. Difference absorption spectra of Rps. rutila membranes indicate that there is no tetraheme reaction center cytochrome c , such as is characteristic of Rps. viridis . However, there are a high potential cytochrome c and a low potential cytochrome b in the membrane, which are suggestive of a cytochrome bc 1 complex. Rps. rutila is most similar to Rps. palustris in microbiological properties, yet it does not have the Cytochromes c -556, c -554, and c -551 in addition to c 2 and c ′, which are characteristic of Rps. palustris . Furthermore, the Rps. rutila cytochrome c ′ is dimeric, whereas the same protein from Rps. palustris is the only one known to be monomeric. The cytochrome pattern is more like that of Rhodospirillum rubrum and Rb. capsulatus , which are apparently only able to make Cytochromes c 2 and c ′.
Mireille Bruschi - One of the best experts on this subject based on the ideXlab platform.
-
Interaction and electron transfer between the high molecular weight cytochrome and cytochrome c3 from Desulfovibrio vulgaris Hildenborough: kinetic, microcalorimetric, EPR and electrochemical studies.
Biochimica et biophysica acta, 2005Co-Authors: Marianne Guiral, Mireille Bruschi, Pierre Bianco, Bruno Guigliarelli, Wolfgang Nitschke, Gisèle Leroy, Philippe Gallice, Marie-thérèse Giudici-orticoniAbstract:The complex formation between the tetraheme cytochrome c3 and hexadecaheme high molecular weight cytochrome c (Hmc), the structure of which has recently been resolved, has been characterized by cross-linking experiments, EPR, electrochemistry and kinetic analysis, and some key parameters of the interaction were determined. The analysis of electron transfer between [Fe] hydrogenase, cytochrome c3 and Hmc demonstrates a redox-shuttling role of cytochrome c3 in the pathway from hydrogenase to Hmc, and shows an effect of redox state on the interaction between the two Cytochromes. The role of polyheme Cytochromes in electron transfer from periplasmic hydrogenase to membrane redox proteins is assessed. A model with cytochrome c3 as an intermediate between hydrogenase and various polyheme Cytochromes is proposed and its physiological consequences are discussed.
-
conformational properties of multihemic Cytochromes c from desulfuromonas acetoxidans
Thermochimica Acta, 2003Co-Authors: M T Giudiciorticoni, V M Lobachov, I I Protasevich, D Lexa, A. A. Makarov, Mireille BruschiAbstract:Abstract In the classification of c-type Cytochromes, the class III includes multihemic Cytochromes c with low redox potential constituting the cytochrome c3 superfamily. Most of the Cytochromes described have been isolated from sulfate or sulfur reducing bacteria. We report here the comparison between two multihemic Cytochromes, the newly characterized 50 kDa cytochrome from Desulfuromonas acetoxidans and the cytochrome c7 from the same strain in order to contribute to understanding the relationships between members of this superfamily. The thermostability of these Cytochromes was studied by circular dichroism (CD) and differential scanning calorimetry (DSC). The influence of the temperature on the redox potential was also investigated. The data clearly indicate the presence of two domains in 50 kDa cytochrome and a drastic loss of stability of cytochrome c7 in comparison to cytochrome c3. The results are discussed in the light of the structural properties of the cytochrome c3 superfamily and two sub-groups in this family are proposed.
-
resonance raman study of multihemic c type Cytochromes from desulfuromonas acetoxidans
FEBS Journal, 2000Co-Authors: Genevia Ve Chottard, Irina Kazanskaya, Mireille BruschiAbstract:Two multihemic Cytochromes c from the sulfur reducing bacteria Desulfuromonas acetoxidans have been studied by optical and resonance Raman spectroscopy: cytochrome c551.5, a trihemic cytochrome and cytochrome c Mr 50 000, a recently isolated high molecular mass cytochrome. The redox and Raman characteristics of cytochrome c551.5 are compared to those of the tetrahemic Cytochromes c3 from Desulfovibrio. While the redox behavior, followed by spectroelectrochemistry, is similar to that of cytochrome c3, showing the same conformational change after reduction of the highest potential heme, the Raman data show a contribution from a His− form of the axial ligands and lead to the assignment of a band at 218 cm−1 to the Fe(III)–(His)2 stretching vibration. The Raman data on cytochrome c Mr 50 000 are in favor of an entirely low spin species with two different sets of axial ligands. A partially reduced state is easily accessible by ascorbate addition.
-
Resonance Raman study of multihemic c‐type Cytochromes from Desulfuromonas acetoxidans
FEBS Journal, 2000Co-Authors: Genevia Ve Chottard, Irina Kazanskaya, Mireille BruschiAbstract:Two multihemic Cytochromes c from the sulfur reducing bacteria Desulfuromonas acetoxidans have been studied by optical and resonance Raman spectroscopy: cytochrome c551.5, a trihemic cytochrome and cytochrome c Mr 50 000, a recently isolated high molecular mass cytochrome. The redox and Raman characteristics of cytochrome c551.5 are compared to those of the tetrahemic Cytochromes c3 from Desulfovibrio. While the redox behavior, followed by spectroelectrochemistry, is similar to that of cytochrome c3, showing the same conformational change after reduction of the highest potential heme, the Raman data show a contribution from a His− form of the axial ligands and lead to the assignment of a band at 218 cm−1 to the Fe(III)–(His)2 stretching vibration. The Raman data on cytochrome c Mr 50 000 are in favor of an entirely low spin species with two different sets of axial ligands. A partially reduced state is easily accessible by ascorbate addition.
-
A sequential electron transfer from hydrogenases to Cytochromes in sulfate-reducing bacteria
Biochimica et Biophysica Acta, 2000Co-Authors: Corinne Aubert, Myriam Brugna, Mireille Bruschi, Alain Dolla, Marie-thérèse Giudici-orticoniAbstract:Abstract A central step in the energy metabolism of sulfate-reducing bacteria is the oxidation of molecular hydrogen, catalyzed by a periplasmic hydrogenase. The resulting electrons are then transferred to various electron transport chains and used for cytoplasmic sulfate reduction. The complex formation between [NiFeSe] hydrogenase and the soluble periplasmic polyheme Cytochromes from Desulfomicrobium norvegicum was characterized by cross-linking experiments, BIAcore and kinetics analysis. Analysis of electron transfer between [NiFeSe] hydrogenase and octaheme cytochrome c3 (Mr 26 000) pointed out that this cytochrome is reduced faster in the presence of catalytic amounts of tetraheme cytochrome c3 (Mr 13 000) isolated from the same organism. The activation of the hydrogenase-dependent reduction of polyheme Cytochromes by cytochrome c3 (Mr 13 000), which is now described in both Desulfovibrio and Desulfomicrobium, is proposed as a general mechanism. During this process, cytochrome c3 (Mr 13 000) would act as an electron shuttle in between hydrogenase and the polyheme Cytochromes and its conductivity appears to be an important factor.
J. Van Beeumen - One of the best experts on this subject based on the ideXlab platform.
-
identification of 42 possible cytochrome c genes in the shewanella oneidensis genome and characterization of six soluble Cytochromes
Omics A Journal of Integrative Biology, 2004Co-Authors: T E Meyer, A I Tsapin, Isabel Vandenberghe, Kenneth H Nealson, Michael A Cusanovich, Lina De Smet, Dmitrij Frishman, J. Van BeeumenAbstract:Through pattern matching of the cytochrome c heme-binding site (CXXCH) against the genome sequence of Shewanella oneidensis MR-1, we identified 42 possible cytochrome c genes (27 of which should be soluble) out of a total of 4758. However, we found only six soluble Cytochromes c in extracts of S. oneidensis grown under several different conditions: (1) a small tetraheme cytochrome c, (2) a tetraheme flavocytochrome c-fumarate reductase, (3) a diheme cytochrome c4, (4) a monoheme cytochrome c5, (5) a monoheme cytochrome c', and (6) a diheme bacterial cytochrome c peroxidase. These Cytochromes were identified either through N-terminal or complete amino acid sequence determination combined with mass spectroscopy. All six Cytochromes were about 10-fold more abundant when cells were grown at low than at high aeration, whereas the flavocytochrome c-fumarate reductase was specifically induced by anaerobic growth on fumarate. When adjusted for the different heme content, the monoheme cytochrome c5 is as abundant as are the small tetraheme cytochrome and the tetraheme fumarate reductase. Published results on regulation of Cytochromes from DNA microarrays and 2D-PAGE differ somewhat from our results, emphasizing the importance of multifaceted analyses in proteomics.
-
Structure and Characterization of Ectothiorhodospira vacuolata Cytochrome b 558, a Prokaryotic Homologue of Cytochrome b 5
The Journal of biological chemistry, 1999Co-Authors: Vesna Kostanjevecki, G. Van Driessche, Terrance E. Meyer, Michael A Cusanovich, D. Leys, Ulrich Fischer, Yves Guisez, J. Van BeeumenAbstract:Abstract A soluble cytochrome b 558from the purple phototropic bacterium Ectothiorhodospira vacuolata was completely sequenced by a combination of automated Edman degradation and mass spectrometry. The protein, with a measured mass of 10,094.7 Da, contains 90 residues and binds a single protoheme. Unexpectedly, the sequence shows homology to eukaryotic Cytochromesb 5. As no prokaryotic homologue had been reported so far, we developed a protocol for the expression, purification, and crystallization of recombinant cytochromeb 558. The structure was solved by molecular replacement to a resolution of 1.65 A. It shows that cytochromeb 558 is indeed the first bacterial cytochromeb 5 to be characterized and differs from its eukaryotic counterparts by the presence of a disulfide bridge and a four-residue insertion in front of the sixth ligand (histidine). Eukaryotes contain a variety of b 5 homologues, including soluble and membrane-bound multifunctional proteins as well as multidomain enzymes such as sulfite oxidase, fatty-acid desaturase, nitrate reductase, and lactate dehydrogenase. A search of theMycobacterium tuberculosis genome showed that a previously unidentified gene encodes a fatty-acid desaturase with an N-terminalb 5 domain. Thus, it may provide another example of a bacterial b 5 homologue.
-
Electron transfer proteins of the purple phototrophic bacterium, Rhodopseudomonas rutila.
Archives of Biochemistry and Biophysics, 1991Co-Authors: R. G. Bartsch, U. Fischer, G. Van Driessche, J. Van Beeumen, J. Fitch, T E Meyer, Michael A CusanovichAbstract:Abstract The soluble electron transfer protein content of Rhodopseudomonas rutila was found to consist of two basic Cytochromes and a (4Fe-4S) ferredoxin. Cytochrome c ′ was easily identified by its characteristic high spin absorption spectra. The native molecular weight is 29,000 and the subunit is 14,000. Cytochrome c -550 has low spin absorption spectra and a high redox potential (376 mV) typical of Cytochromes c 2 . The molecular weight is about 14,000. The ferredoxin is apparently a dimer (43,000) of approximately 18,000 Da subunits. There are 1.3 to 1.5 iron-sulfur clusters per monomer of 18-to 21-kDa protein. The N-terminal amino acid sequence is like the (7Fe-8S) ferredoxins of Rhodobacter capsulatus and Azotobacter vinelandii . Remarkably, there are only 2 or 3 out of 25 amino acid substitutions. Difference absorption spectra of Rps. rutila membranes indicate that there is no tetraheme reaction center cytochrome c , such as is characteristic of Rps. viridis . However, there are a high potential cytochrome c and a low potential cytochrome b in the membrane, which are suggestive of a cytochrome bc 1 complex. Rps. rutila is most similar to Rps. palustris in microbiological properties, yet it does not have the Cytochromes c -556, c -554, and c -551 in addition to c 2 and c ′, which are characteristic of Rps. palustris . Furthermore, the Rps. rutila cytochrome c ′ is dimeric, whereas the same protein from Rps. palustris is the only one known to be monomeric. The cytochrome pattern is more like that of Rhodospirillum rubrum and Rb. capsulatus , which are apparently only able to make Cytochromes c 2 and c ′.
A I Tsapin - One of the best experts on this subject based on the ideXlab platform.
-
identification of 42 possible cytochrome c genes in the shewanella oneidensis genome and characterization of six soluble Cytochromes
Omics A Journal of Integrative Biology, 2004Co-Authors: T E Meyer, A I Tsapin, Isabel Vandenberghe, Kenneth H Nealson, Michael A Cusanovich, Lina De Smet, Dmitrij Frishman, J. Van BeeumenAbstract:Through pattern matching of the cytochrome c heme-binding site (CXXCH) against the genome sequence of Shewanella oneidensis MR-1, we identified 42 possible cytochrome c genes (27 of which should be soluble) out of a total of 4758. However, we found only six soluble Cytochromes c in extracts of S. oneidensis grown under several different conditions: (1) a small tetraheme cytochrome c, (2) a tetraheme flavocytochrome c-fumarate reductase, (3) a diheme cytochrome c4, (4) a monoheme cytochrome c5, (5) a monoheme cytochrome c', and (6) a diheme bacterial cytochrome c peroxidase. These Cytochromes were identified either through N-terminal or complete amino acid sequence determination combined with mass spectroscopy. All six Cytochromes were about 10-fold more abundant when cells were grown at low than at high aeration, whereas the flavocytochrome c-fumarate reductase was specifically induced by anaerobic growth on fumarate. When adjusted for the different heme content, the monoheme cytochrome c5 is as abundant as are the small tetraheme cytochrome and the tetraheme fumarate reductase. Published results on regulation of Cytochromes from DNA microarrays and 2D-PAGE differ somewhat from our results, emphasizing the importance of multifaceted analyses in proteomics.
-
identification of 42 possible cytochrome c genes in the shewanella oneidensis genome and characterization of six soluble Cytochromes
Omics A Journal of Integrative Biology, 2004Co-Authors: T E Meyer, A I Tsapin, Isabel Vandenberghe, Kenneth H Nealson, Michael A Cusanovich, Lina De Smet, Dmitrij Frishman, Jozef Van BeeumenAbstract:Through pattern matching of the cytochrome c heme-binding site (CXXCH) against the genome sequence of Shewanella oneidensis MR-1, we identified 42 possible cytochrome c genes (27 of which should be soluble) out of a total of 4758. However, we found only six soluble Cytochromes c in extracts of S. oneidensis grown under several different conditions: (1) a small tetraheme cytochrome c, (2) a tetraheme flavocytochrome c-fumarate reductase, (3) a diheme cytochrome c4, (4) a monoheme cytochrome c5, (5) a monoheme cytochrome c′, and (6) a diheme bacterial cytochrome c peroxidase. These Cytochromes were identified either through N-terminal or complete amino acid sequence determination combined with mass spectroscopy. All six Cytochromes were about 10-fold more abundant when cells were grown at low than at high aeration, whereas the flavocytochrome c-fumarate reductase was specifically induced by anaerobic growth on fumarate. When adjusted for the different heme content, the monoheme cytochrome c5 is as abundant ...
-
identification of a small tetraheme cytochrome c and a flavocytochrome c as two of the principal soluble Cytochromes c in shewanella oneidensis strain mr1
Applied and Environmental Microbiology, 2001Co-Authors: A I Tsapin, Isabel Vandenberghe, Kenneth H Nealson, J H Scott, T E Meyer, Michael A Cusanovich, E Harada, T Kaizu, Hideo Akutsu, David LeysAbstract:Two abundant, low-redox-potential Cytochromes c were purified from the facultative anaerobe Shewanella oneidensis strain MR1 grown anaerobically with fumarate. The small cytochrome was completely sequenced, and the genes coding for both proteins were cloned and sequenced. The small cytochrome c contains 91 residues and four heme binding sites. It is most similar to the Cytochromes c from Shewanella frigidimarina (formerly Shewanella putrefaciens) NCIMB400 and the unclassified bacterial strain H1R (64 and 55% identity, respectively). The amount of the small tetraheme cytochrome is regulated by anaerobiosis, but not by fumarate. The larger of the two low-potential Cytochromes contains tetraheme and flavin domains and is regulated by anaerobiosis and by fumarate and thus most nearly corresponds to the flavocytochrome c-fumarate reductase previously characterized from S. frigidimarina to which it is 59% identical. However, the genetic context of the cytochrome genes is not the same for the two Shewanella species, and they are not located in multicistronic operons. The small cytochrome c and the cytochrome domain of the flavocytochrome c are also homologous, showing 34% identity. Structural comparison shows that the Shewanella tetraheme Cytochromes are not related to the Desulfovibrio Cytochromes c3 but define a new folding motif for small multiheme Cytochromes c.
