Characterization of the Cytochromes C fromDesulfovibrio desulfuricansG201

Aubert, Corinne; Leroy, Gisèle; Bianco, Pierre; Forest, Éric; Bruschi, Mireille; Dolla, Alain

doi:10.1006/bbrc.1997.7852

Cited by 20 publications

(10 citation statements)

References 31 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The N-terminal 20 amino acids of the mature cytochrome c 3 reported for this strain (32) correlate exactly with residues 24 through 43 of the deduced polypeptide, confirming the identity of the cycA gene. The 21st residue, reported from the protein sequencing to be a lysine (32), was found instead from the gene sequence to be a histidine, confirming the more recent protein sequencing of Aubert et al (3). When compared with tetraheme cytochromes from several other Desulfovibrio strains (Fig.…”

Section: Resultssupporting

confidence: 77%

See 1 more Smart Citation

Cytochrome c ₃ Mutants of Desulfovibrio desulfuricans

Casalot

et al. 2000

Appl Environ Microbiol

View full text Add to dashboard Cite

To explore the physiological role of tetraheme cytochrome c 3 in the sulfate-reducing bacterium Desulfovibrio desulfuricans G20, the gene encoding the preapoprotein was cloned, sequenced, and mutated by plasmid insertion. The physical analysis of the DNA from the strain carrying the integrated plasmid showed that the insertion was successful. The growth rate of the mutant on lactate with sulfate was comparable to that of the wild type; however, mutant cultures did not achieve the same cell densities. Pyruvate, the oxidation product of lactate, served as a poor electron source for the mutant. Unexpectedly, the mutant was able to grow on hydrogensulfate medium. These data support a role for tetraheme cytochrome c 3 in the electron transport pathway from pyruvate to sulfate or sulfite in D. desulfuricans G20.The anaerobic sulfate-reducing bacteria have several lowpotential c-type cytochromes that are located in the periplasm and presumably function in electron transfer events. Several members of the genus Desulfovibrio have been shown to have three cytochromes in this class, monoheme cytochrome c 553 , tetraheme cytochrome c 3 , and a high-molecular-weight cytochrome c (Hmc) with 16 hemes (20,21). Of these cytochromes, the most abundant, and that for which the most structural information has been gathered, is tetraheme cytochrome c 3 (8, 21).The physiological role of tetraheme cytochrome c 3 remains enigmatic. This cytochrome has been reported to interact effectively with an almost unrealistic list of electron donors and acceptors. In vivo, c 3 has been suggested to be the redox partner of the periplasmic hydrogenases (5, 22), a role supported by the finding that this cytochrome is tightly associated with hydrogenases during purification of the latter (17). A model in which tetraheme cytochrome c 3 shuttles electrons from hydrogenases to the various polyheme cytochromes (Hmc, nineheme cytochrome, or octaheme cytochrome c 3 ) has been proposed (2,15,18). In addition to having periplasmically located redox partners, tetraheme cytochrome c has been shown to form functional complexes with a number of cytosolic electron carriers, including ferredoxin (9), rubredoxin (28), and flavodoxin (16). In vitro studies have shown that tetraheme cytochrome c 3 and an [NiFe] hydrogenase will mediate reduction of metals, including Fe(III), Cr(VI), and U(VI), with hydrogen as the electron donor (13).The reactive nature of tetraheme cytochrome c 3 makes biochemical characterization of redox partners and functional analysis problematic; therefore, a genetic approach was initiated. As a first step, it was necessary to determine whether this cytochrome is essential for cell growth. Construction of a strain with an interrupted gene encoding tetraheme cytochrome c 3 (cycA) allowed confirmation that this cytochrome is not required for growth with lactate as the primary source of carbon and reductant and with sulfate as the terminal electron acceptor. However, the mutant grew poorly, if at all, on pyruvatesulfate medium. We infer that the fi...

show abstract

Section: Resultssupporting

confidence: 77%

“…For the identification of cycA, the derived amino acid sequences were compared to protein sequences in GenBank. Twenty of the amino acid residues reported for the purified mature cytochrome c 3 (32) were found to be part of the deduced polypeptide, confirming the identification of cycA.…”

supporting

confidence: 72%

Cytochrome c ₃ Mutants of Desulfovibrio desulfuricans

Casalot

et al. 2000

Appl Environ Microbiol

View full text Add to dashboard Cite

show abstract

“…For example, bacterial c-type cytochromes undergo a complex post-translational maturation process involving covalent attachment of haem groups. This modification can change the charge state in the gas phase and cause atypical fragmentation of peptides, resulting in loss of detection by current proteomics technology (Aubert et al, 1998). By using the integrated 'omics' approach, the expression of c-type cytochromes involved in electrontransport processes was demonstrated in Desulfovibrio vulgaris (Nie et al, 2006c;Zhang et al, 2006a, b).…”

Section: Integrated Transcriptomics and Proteomicsmentioning

confidence: 99%

Integrating multiple ‘omics’ analysis for microbial biology: application and methodologies

Zhang

Li²,

Nie³

2010

Microbiology

410

241

View full text Add to dashboard Cite

Recent advances in various ‘omics’ technologies enable quantitative monitoring of the abundance of various biological molecules in a high-throughput manner, and thus allow determination of their variation between different biological states on a genomic scale. Several popular ‘omics’ platforms that have been used in microbial systems biology include transcriptomics, which measures mRNA transcript levels; proteomics, which quantifies protein abundance; metabolomics, which determines abundance of small cellular metabolites; interactomics, which resolves the whole set of molecular interactions in cells; and fluxomics, which establishes dynamic changes of molecules within a cell over time. However, no single ‘omics’ analysis can fully unravel the complexities of fundamental microbial biology. Therefore, integration of multiple layers of information, the multi-‘omics’ approach, is required to acquire a precise picture of living micro-organisms. In spite of this being a challenging task, some attempts have been made recently to integrate heterogeneous ‘omics’ datasets in various microbial systems and the results have demonstrated that the multi-‘omics’ approach is a powerful tool for understanding the functional principles and dynamics of total cellular systems. This article reviews some basic concepts of various experimental ‘omics’ approaches, recent application of the integrated ‘omics’ for exploring metabolic and regulatory mechanisms in microbes, and advances in computational and statistical methodologies associated with integrated ‘omics’ analyses. Online databases and bioinformatic infrastructure available for integrated ‘omics’ analyses are also briefly discussed.

show abstract

“…1 and Supplementary Table 1 online). The tetrahemic cytochrome c 3 (DVU3171) is generally regarded as the primary electron acceptor from periplasmic hydrogen oxidation and accounts for the majority of the c-type cytochromes of the periplasm 14 . However, genome analysis indicates the presence of three alternate c 3 -type cytochromes (DVU2524, DVU2809 and DVU0263); localization of two of these (DVU2524 and DVU2809) suggests roles in dedicated pathways.…”

Section: Energy Metabolismmentioning

confidence: 99%

The genome sequence of the anaerobic, sulfate-reducing bacterium Desulfovibrio vulgaris Hildenborough

Heidelberg¹,

Seshadri²,

et al. 2004

View full text Add to dashboard Cite

Sulfate-reducing bacteria (SRB) are anaerobic prokaryotes found ubiquitously in nature. SRB were the first nonphotosynthetic, anaerobic bacteria shown to generate energy (ATP) through electron transfer-coupled phosphorylation. For this process, the SRB typically use sulfate as the terminal electron acceptor for respiration of hydrogen or various organic acids, which results in the production of sulfide, a highly reactive and toxic end-product. Beyond their obvious function in the sulfur cycle, SRB play an important role in global cycling of numerous other elements 1 . For example, in the carbon cycle, the SRB form part of microbial consortia that completely mineralize organic carbon in anaerobic environments; polymeric materials (e.g., cellulose) are first depolymerized and metabolized by fermentative microorganisms, and the resulting organic acid and reduced gas (that is, CO and H 2 ) end-products are further fermented or oxidized by other microbes, including SRB. The latter are particularly active in sulfate-rich (e.g., marine) environments, where they effectively link the global sulfur and carbon cycles 1,2 .Beyond these ecological roles, SRB also have a major economic impact because of their involvement in biocorrosion of ferrous metals in anaerobic environments 3 , described as "industrial venereal disease-it's expensive, everybody has it, and nobody wants to talk about it" 4 . For example, because SRB are abundant in oil fields, their metabolism has many negative consequences for the petroleum industry (e.g., corrosion of drilling and pumping machinery and storage tanks, souring of oil by sulfide production, plugging of machinery and rock pores with biomass and sulfide precipitates). The SRB also contribute to bioremediation of toxic metal ions 5,6 . Their metabolism increases the pH, causing toxic metal ions like copper (II), nickel (II) and cadmium (II) to precipitate as metal sulfides in acidic aquatic environments (e.g., mine effluents). Additionally, SRB can deliver electrons directly to oxidized toxic metal ions, including uranium (VI), technetium (VII), and chromium (VI), converting these into less soluble, reduced forms. Hence, SRB-mediated reduction represents a potentially useful mechanism for the bioremediation of metal ion contaminants from anaerobic sediments 6 .Most research on the metabolism and biochemistry of SRB has been done on the genus Desulfovibrio, a member of the δ-proteobacteria The genome sequence of the anaerobic, sulfate-reducing bacterium Desulfovibrio vulgaris Hildenborough Desulfovibrio vulgaris Hildenborough is a model organism for studying the energy metabolism of sulfate-reducing bacteria (SRB) and for understanding the economic impacts of SRB, including biocorrosion of metal infrastructure and bioremediation of toxic metal ions. The 3,570,858 base pair (bp) genome sequence reveals a network of novel c-type cytochromes, connecting multiple periplasmic hydrogenases and formate dehydrogenases, as a key feature of its energy metabolism. The relative arrangement of genes encod...

show abstract

Characterization of the Cytochromes C fromDesulfovibrio desulfuricansG201

Cited by 20 publications

References 31 publications

Cytochrome c ₃ Mutants of Desulfovibrio desulfuricans

Cytochrome c ₃ Mutants of Desulfovibrio desulfuricans

Integrating multiple ‘omics’ analysis for microbial biology: application and methodologies

The genome sequence of the anaerobic, sulfate-reducing bacterium Desulfovibrio vulgaris Hildenborough

Contact Info

Product

Resources

About

Characterization of the Cytochromes C fromDesulfovibrio desulfuricansG201

Cited by 20 publications

References 31 publications

Cytochrome c 3 Mutants of Desulfovibrio desulfuricans

Cytochrome c 3 Mutants of Desulfovibrio desulfuricans

Integrating multiple ‘omics’ analysis for microbial biology: application and methodologies

The genome sequence of the anaerobic, sulfate-reducing bacterium Desulfovibrio vulgaris Hildenborough

Contact Info

Product

Resources

About

Cytochrome c ₃ Mutants of Desulfovibrio desulfuricans

Cytochrome c ₃ Mutants of Desulfovibrio desulfuricans