Redox-Bohr effect in electron/proton energy transduction: cytochrome c 3 coupled to hydrogenase works as a 'proton thruster' in Desulfovibrio vulgaris

1997 ◽  
Vol 2 (4) ◽  
pp. 488-491 ◽  
Author(s):  
Ricardo O. Louro ◽  
Teresa Catarino ◽  
Jean LeGall ◽  
António V. Xavier
Keyword(s):  
Cytochrome C ◽  
Proton Energy ◽  
Energy Transduction ◽  
Bohr Effect ◽  
Desulfovibrio Vulgaris ◽  
Redox Bohr Effect

Theoretical studies on the redox-Bohr effect in cytochrome c 3 from Desulfovibrio vulgaris Hildenborough

1997 ◽  
Vol 2 (6) ◽  
pp. 714-727 ◽  
Author(s):  
Cláudio M. Soares ◽  
Paulo J. Martel ◽  
Maria A. Carrondo
Keyword(s):  
Cytochrome C ◽  
Bohr Effect ◽  
Desulfovibrio Vulgaris ◽  
Theoretical Studies ◽  
Desulfovibrio Vulgaris Hildenborough ◽  
Redox Bohr Effect

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 Amino acid sequence of cytochrome c-553 from Desulfovibrio vulgaris Miyazaki.

1983 ◽  
Vol 258 (20) ◽  
pp. 12409-12412
Author(s):  
K Nakano ◽  
Y Kikumoto ◽  
T Yagi
Keyword(s):  
Amino Acid ◽  
Cytochrome C ◽  
Amino Acid Sequence ◽  
Desulfovibrio Vulgaris

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 The haem–copper oxygen reductase of Desulfovibrio vulgaris contains a dihaem cytochrome c in subunit II

2008 ◽  
Vol 1777 (12) ◽  
pp. 1528-1534 ◽  
Author(s):  
Susana A.L. Lobo ◽  
Claúdia C. Almeida ◽  
João N. Carita ◽  
Miguel Teixeira ◽  
Lígia M. Saraiva
Keyword(s):  
Cytochrome C ◽  
Desulfovibrio Vulgaris ◽  
Oxygen Reductase

Crystallization And Mad Data Collection Of High-Molecular Weight Cytochrome C From Desulfovibrio Vulgaris Miyazaki F

2004 ◽  
Vol 11 (1) ◽  
pp. 93-96
Author(s):  
Naoki Shibata ◽  
Kyoko Suto ◽  
Eiko Ichimura ◽  
Kazutaka Yoshimura ◽  
Kenji Muneo ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Cytochrome C ◽  
Data Collection ◽  
High Molecular Weight ◽  
Desulfovibrio Vulgaris

scholarly journals Effect of 3,5-di-iodo-L-thyronine on the mitochondrial energy-transduction apparatus

1998 ◽  
Vol 330 (1) ◽  
pp. 521-526 ◽  
Author(s):  
Assonta LOMBARDI ◽  
Antonia LANNI ◽  
Maria MORENO ◽  
D. Martin BRAND ◽  
Fernando GOGLIA
Keyword(s):  
Cytochrome C ◽  
Mitochondrial Respiration ◽  
Atp Synthesis ◽  
Substrate Oxidation ◽  
Energy Transduction ◽  
Energy Utilization ◽  
Proton Leak ◽  
Elasticity Analysis ◽  
Top Down ◽  
Respiratory State

We examined the effect of a single injection of 3,5-di-iodo-l-thyronine (3,5-T2) (150 μg/100 g body weight) on the rat liver mitochondrial energy-transduction apparatus. We applied ‘top-down’ elasticity analysis, which allows identification of the site of action of an effector within a metabolic pathway. This kinetic approach considers oxidative phosphorylation as two blocks of reactions: those generating the mitochondrial inner-membrane potential (Δψ; ‘substrate oxidation’) and those ‘consuming’ it (‘proton leak’ and ‘phosphorylating system’). The results show that 1 h after the injection of 3,5-T2, state 4 (respiratory state in which there is no ATP synthesis and the exogenous ADP added has been exhausted) and state 3 (respiratory state in which ATP synthesis is at maximal rate) of mitochondrial respiration were significantly increased (by approx. 30%). ‘Top-down’ elasticity analysis revealed that these increases were due to the stimulation of reactions involved in substrate oxidation; neither ‘proton leak’ nor the ‘phosphorylating system’ was influenced by 3,5-T2. Using the same approach we divided the respiratory chain into two blocks of reactions: cytochrome c reducers and cytochrome c oxidizers. We found that both cytochrome c reducers and cytochrome c oxidizers are targets for 3,5-T2. The rapidity with which 3,5-T2 acts in stimulating the mitochondrial respiration rate suggests to us that di-iodo-L-thyronine may play an important role in the physiological conditions in which rapid energy utilization is required, such as cold exposure or overfeeding.

S-Class Cytochromes c Have a Variety of Folding Patterns: Structure of Cytochrome c-553 from Desulfovibrio vulgaris Determined by the Multi-Wavelength Anomalous Dispersion Method1

1990 ◽  
Vol 108 (5) ◽  
pp. 701-703 ◽  
Author(s):  
Atsushi Nakagawa ◽  
Yoshiki Higuchi ◽  
Noritake Yasuoka ◽  
Yukiteru Katsube ◽  
Tatsuhiko Yagi
Keyword(s):  
Cytochrome C ◽  
Anomalous Dispersion ◽  
Desulfovibrio Vulgaris ◽  
Cytochromes C ◽  
Multi Wavelength
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