Redox-Bohr effect in the tetrahaem cytochrome c3 from Desulfovibrio vulgaris: a model for energy transduction mechanisms

1996 ◽  
Vol 1 (1) ◽  
pp. 34-38 ◽  
Author(s):  
Ricardo O. Louro ◽  
Teresa Catarino ◽  
Carlos A. Salgueiro ◽  
Jean LeGall ◽  
António V. Xavier
Keyword(s):  
Energy Transduction ◽  
Bohr Effect ◽  
Desulfovibrio Vulgaris ◽  
Cytochrome C3 ◽  
Transduction Mechanisms ◽  
Redox Bohr Effect

scholarly journals Exploring Coupled Redox and pH Processes with a Force Field-Based Approach: Applications to Five Different Systems

2020 ◽  
Author(s):  
Vinicius Cruzeiro ◽  
Gustavo Troiano Feliciano ◽  
Adrian Roitberg
Keyword(s):  
Force Field ◽  
Redox Potential ◽  
Desulfovibrio Vulgaris ◽  
Cytochrome C3 ◽  
Computational Tools ◽  
Redox States ◽  
Computational Performance ◽  
Redox Active ◽  
Constant Ph ◽  
Experimental Findings

Coupled redox and pH-driven processes are at the core of many important biological mechanisms. As the distribution of protonation and redox states in a system is associated with the pH and redox potential of the solution, having efficient computational tools that can simulate under these conditions become very important. Such tools have the potential to provide information that complement and drive experiments. In previous publications we have presented the implementation of the constant pH and redox potential molecular dynamics (C(pH,E)MD) method in AMBER and we have shown how multidimensional replica exchange can be used to significantly enhance the convergence efficiency of our simulations. In the current work, after an improvement in our C(pH,E)MD approach that allows a given residue to be simultaneously pH- and redox-active, we have employed our methodologies to study five different systems of interest in the literature. We present results for: capped tyrosine dipeptide, two maquette systems containing one pH- and redox-active tyrosine (α3Y and peptide A), and two proteins that contain multiple heme groups (diheme cytochrome c from Rhodobacter sphaeroides and Desulfovibrio vulgaris Hildenborough cytochrome c3). We show that our results can provide new insights into previous theoretical and experimental findings by using a fully force field-based and GPUaccelerated approach, which allows the simulations to be executed with high computational performance.

scholarly journals Fine Tuning of Redox Networks on Multiheme Cytochromes fromGeobacter sulfurreducensDrives Physiological Electron/Proton Energy Transduction

2012 ◽  
Vol 2012 ◽  
pp. 1-9 ◽  
Author(s):  
Leonor Morgado ◽  
Joana M. Dantas ◽  
Marta Bruix ◽  
Yuri Y. Londer ◽  
Carlos A. Salgueiro
Keyword(s):  
Microbial Fuel Cells ◽  
Geobacter Sulfurreducens ◽  
Cellular Growth ◽  
Bohr Effect ◽  
Fine Tuning ◽  
Physiological Relevance ◽  
Ph Range ◽  
Coupling Mechanisms ◽  
Redox Bohr Effect

The bacteriumGeobacter sulfurreducens (Gs)can grow in the presence of extracellular terminal acceptors, a property that is currently explored to harvest electricity from aquatic sediments and waste organic matter into microbial fuel cells. A family composed of five triheme cytochromes (PpcA-E) was identified inGs. These cytochromes play a crucial role by bridging the electron transfer from oxidation of cytoplasmic donors to the cell exterior and assisting the reduction of extracellular terminal acceptors. The detailed thermodynamic characterization of such proteins showed that PpcA and PpcD have an important redox-Bohr effect that might implicate these proteins in the e−/H+coupling mechanisms to sustain cellular growth. The physiological relevance of the redox-Bohr effect in these proteins was studied by determining the fractional contribution of each individual redox-microstate at different pH values. For both proteins, oxidation progresses from a particular protonated microstate to a particular deprotonated one, over specific pH ranges. The preferred e−/H+transfer pathway established by the selected microstates indicates that both proteins are functionally designed to couple e−/H+transfer at the physiological pH range for cellular growth.

scholarly journals Uranium Reduction by Desulfovibrio desulfuricans Strain G20 and a Cytochrome c3 Mutant

2002 ◽  
Vol 68 (6) ◽  
pp. 3129-3132 ◽  
Author(s):  
Rayford B. Payne ◽  
Darren M. Gentry ◽  
Barbara J. Rapp-Giles ◽  
Laurence Casalot ◽  
Judy D. Wall
Keyword(s):  
Electron Donor ◽  
Desulfovibrio Desulfuricans ◽  
Desulfovibrio Vulgaris ◽  
In Vitro Experiments ◽  
Wild Type ◽  
Cytochrome C3 ◽  
Uranium Reduction

ABSTRACT Previous in vitro experiments with Desulfovibrio vulgaris strain Hildenborough demonstrated that extracts containing hydrogenase and cytochrome c 3 could reduce uranium(VI) to uranium(IV) with hydrogen as the electron donor. To test the involvement of these proteins in vivo, a cytochrome c 3 mutant of D. desulfuricans strain G20 was assayed and found to be able to reduce U(VI) with lactate or pyruvate as the electron donor at rates about one-half of those of the wild type. With electrons from hydrogen, the rate was more severely impaired. Cytochrome c 3 appears to be a part of the in vivo electron pathway to U(VI), but additional pathways from organic donors can apparently bypass this protein.

Identification of the genes for hydrogenase and cytochrome c3 in Desulfovibrio

1987 ◽  
Vol 33 (11) ◽  
pp. 1006-1010 ◽  
Author(s):  
Gerrit Voordouw ◽  
Helen M. Kent ◽  
John R. Postgate
Keyword(s):  
Cytochrome C ◽  
Sequence Divergence ◽  
Desulfovibrio Vulgaris ◽  
Gene Probe ◽  
Cytochrome C3 ◽  
Sulfate Reducing ◽  
Genes Encoding ◽  
Reducing Bacteria ◽  
Cryptic Plasmids ◽  
Amino Acid Sequence Divergence

Cloned genes encoding cytochrome c3 and hydrogenase from Desulfovibrio vulgaris Hildenborough have been used to probe the genomes of 15 other desulfovibrios. The D. vulgaris strains Wandle and Brockhurst Hill cannot be distinguished from the Hildenborough strain by Southern hybridization using either probe, indicating similar genomes. Desulfovibrio vulgaris Groningen is completely different and lacks homologous cytochrome c3 and hydrogenase genes. The genomes of D. vulgaris ssp. oxamicus Monticello and D. desulfuricans strains El Agheila Z, Berre sol, and Canet 41 contain genes encoding a homologous but not identical periplasmic hydrogenase and cytochrome c3. Weak hybridization was observed with the cytochrome c3 gene probe for genomes of seven other sulfate-reducing bacteria, which reflects the known amino acid sequence divergence of cytochrome c3 in Desulfovibrio. The hydrogenase gene probe shows weak hybridization to the DNA from two strains of D. salexigens only, while the gene may be absent from D. vulgaris Groningen, two strains of D. africanus, D. thermophilus, D. gigas, and D. desulfuricans strains Norway and Teddington R. In desulfovibrios carrying cryptic plasmids the cytochrome c3 and hydrogenase genes are apparently chromosomal.

scholarly journals EPR study of the redox interactions in cytochrome c3 from Desulfovibrio vulgaris Miyazaki

1989 ◽  
Vol 182 (1) ◽  
pp. 51-55 ◽  
Author(s):  
Hafeda BENOSMAN ◽  
Marcel ASSO ◽  
Patrick BERTRAND ◽  
Tatsuhiko YAGI ◽  
Jean-Pierre GAYDA
Keyword(s):  
Desulfovibrio Vulgaris ◽  
Cytochrome C3
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