Biogenesis of respiratory cytochromes in bacteria.

Thöny-Meyer, L

doi:10.1128/.61.3.337-376.1997

Cited by 286 publications

(128 citation statements)

References 295 publications

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“…1) and confirmed by MALDI-TOF-MS. The peak of the pure cytochrome in the mass spectrum corresponds to a molecular mass of 15 453.05 Da (±0.02%), which is in excellent agreement with the predicted MW for mature PccH with a signal peptide cleavage site after residue 21 (15 452.91 Da, resulting from 14 836.91 Da from the apo-protein plus 616 Da of one heme group [15]). The similarity between the predicted and experimental values also indicates that PccH contains a single heme group, which was further confirmed by the pyridine hemochrome assay.…”

Section: Production Of Cytochrome Pcchsupporting

confidence: 77%

“…The theoretical molecular mass of cytochrome PccH was calculated according to the amino acid composition of the mature protein (http://ca.expasy.org/tools/pi_tool.html) plus the molecular mass of one heme c group [15]. The experimental molecular mass determination and heme quantification of PccH are described in Appendix C (Supplementary methods).…”

Section: Molecular Mass Determination and Heme Quantificationmentioning

confidence: 99%

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Functional characterization of PccH, a key cytochrome for electron transfer from electrodes to the bacterium Geobacter sulfurreducens

et al. 2013

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a b s t r a c tThe cytochrome PccH from Geobacter sulfurreducens (Gs) plays a crucial role in current-consuming fumarate-reducing biofilms. Deletion of pccH gene inhibited completely electron transfer from electrodes toward Gs cells. The pccH gene was cloned and the protein heterologously expressed in Escherichia coli. Complementary biophysical techniques including CD, UV-visible and NMR spectroscopy were used to characterize PccH. This cytochrome contains one low-spin c-type heme with His-Met axial coordination and unusual low-reduction potential. This reduction potential is pH-dependent, within the Gs physiological pH range, and is discussed within the context of the electron transfer mechanisms from electrodes to Gs cells.

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Section: Production Of Cytochrome Pcchsupporting

confidence: 77%

Section: Molecular Mass Determination and Heme Quantificationmentioning

confidence: 99%

Functional characterization of PccH, a key cytochrome for electron transfer from electrodes to the bacterium Geobacter sulfurreducens

et al. 2013

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“…The predicted ShxV was highly homologous to CcdA of P. pantotrophus, essential for cytochrome c biogenesis [9]. Both genes, shxV and ccdA, predicted channel-forming transmembrane proteins homologous to CcdA of Bacillus subtilis, Rhodobacter capsulatus and DipZ of E. coli and Pseudomonas aeruginosa which participate in cytochrome c biogenesis [8]. Disruption of shxV a¡ected exclusively lithotrophic traits but not cytochrome c biogenesis.…”

Section: Discussionmentioning

confidence: 99%

“…DipZ is proposed to be involved in transport of electrons into the periplasm via two conserved cysteines [8,23]. The high structural identity of the predicted shxV gene product with CcdA or DipZ and the neighboring putative thioredoxin ShxW also suggest a function for electron transport which direction is presently unknown.…”

Section: Discussionmentioning

confidence: 99%

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The shxVW locus is essential for oxidation of inorganic sulfur and molecular hydrogen by Paracoccus pantotrophus GB17: a novel function for lithotrophy

Bardischewsky¹

2001

FEMS Microbiology Letters

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The shxVW genes of Paracoccus pantotrophus were identified to be essential for lithotrophic oxidation of sulfur and hydrogen. shxV predicts a membrane protein which is 42% identical to CcdA of P. pantotrophus essential for cytochrome c biogenesis. shxW predicts a periplasmic thioredoxin. Disruption of shxV by an 6-kanamycin interposon disabled the resulting mutant GB6V to grow with thiosulfate or molecular hydrogen and to express ShxW while cytochrome c formation was not affected. Mixotrophic growth with succinate and thiosulfate of strain GB6V revealed 2% of the thiosulfate-dependent oxygen uptake rate as compared to the wild-type while antigens of proteins essential for sulfur oxidation were present in both strains. Mixotrophic growth of strain GB6V with succinate and molecular hydrogen revealed neither hydrogenase activity nor antigens. Complementation analysis with plasmid pBHP6 carrying the shxVW genes revealed the wild-type phenotype of strain GB6V(pBHP6). ß

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Trimethylamine N ‐Oxide Reductase

Iobbi‐Nivol

Haser²,

M��jean

et al. 2004

Handbook of Metalloproteins

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Trimethylamine N ‐oxide (TMAO) is a compound widely distributed in marine fish and invertebrates; and TMAO reducing enzymes are found not only in marine bacteria and photosynthetic bacteria living in ponds but also in enterobacteria. The various respiratory systems reducing TMAO, described so far, share a high level of homology either in their general structure, or in the regulation or mechanism of electron transfer. According to their content of molybdenum cofactor, the enzymes in charge of TMAO reduction are classified in the structural dimethylsulfoxide (DMSO) reductase family. TMAO reductases, however, in contrast to DMSO reductases are highly specific enzymes and reduce only their physiological substrate. The crystal structure was determined for the TMAO reductase from Shewanella massilia , and its structural differences with DMSO reductases in the environment of the active site. A tyrosine residue in the proximity of the molybdenum ion in DMSO reductases is absent in TMAO reductases and could be related to the differences in substrate specificities.

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Biogenesis of respiratory cytochromes in bacteria.

Cited by 286 publications

References 295 publications

Functional characterization of PccH, a key cytochrome for electron transfer from electrodes to the bacterium Geobacter sulfurreducens

Functional characterization of PccH, a key cytochrome for electron transfer from electrodes to the bacterium Geobacter sulfurreducens

The shxVW locus is essential for oxidation of inorganic sulfur and molecular hydrogen by Paracoccus pantotrophus GB17: a novel function for lithotrophy

Trimethylamine N ‐Oxide Reductase

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