DMSO respiration by the anaerobic rumen bacterium Wolinella succinogenes

1994 ◽  
Vol 162 (4) ◽  
pp. 277-281 ◽  
Author(s):  
J�rgen Lorenzen ◽  
Swantje Steinwachs ◽  
Gottfried Unden
Keyword(s):  
Rumen Bacterium ◽  
Wolinella Succinogenes

scholarly journals An analysis of the reaction kinetics of the hexahaem nitrite reductase of the anaerobic rumen bacterium Wolinella succinogenes

1990 ◽  
Vol 271 (2) ◽  
pp. 457-461 ◽  
Author(s):  
R S Blackmore ◽  
T Brittain ◽  
C Greenwood
Keyword(s):  
Electron Transfer ◽  
Reaction Kinetics ◽  
Nitrite Reductase ◽  
Rate Constants ◽  
Rumen Bacterium ◽  
Square Root ◽  
Wolinella Succinogenes ◽  
Single Turnover ◽  
Internal Electron ◽  
Kinetics Of

The reduction kinetics of both the resting and redox-cycled forms of the nitrite reductase from the anaerobic rumen bacterium Wolinella succinogenes were studied by stopped-flow reaction techniques. Single-turnover reduction of the enzyme by dithionite occurs in two kinetic phases for both forms of the enzyme. When the resting form of the enzyme is subjected to a single-turnover reduction by dithionite, the slower of the two kinetic phases exhibits a hyperbolic dependence of the rate constant on the square root of the reductant concentration, the limiting value of which (approximately 4 s-1) is assigned to a slow internal electron-transfer process. In contrast, when the redox-cycled form of the enzyme is reduced by dithionite in a single-turnover experiment, both kinetic phases exhibit linear dependences of the rate on the square root of dithionite concentration, with associated rate constants of 150 M-1/2.s-1 and 6 M-1/2.s-1. Computer simulations of both the reduction processes shows that no unique set of rate constants can account for the kinetics of both forms, although the kinetics of the redox-cycled species is consistent with a much enhanced rate of internal electron transfer. Under turnover conditions the time course for reduction of the enzyme, in the presence of millimolar levels of nitrite and 100 mM-dithionite, is extremely complex. A working model for the mechanism of the turnover activity of the enzyme is proposed which very closely describes the reaction kinetics over a wide range of substrate concentrations, as shown by computer simulation. The similarity in the action of the nitrite reductase enzyme and mammalian cytochrome c oxidase is commented upon.

DMSO respiration by the anaerobic rumen bacterium Wolinella succinogenes

1994 ◽  
Vol 162 (4) ◽  
pp. 277-281
Author(s):  
J�rgen Lorenzen ◽  
Swantje Steinwachs ◽  
G. Unden
Keyword(s):  
Rumen Bacterium ◽  
Wolinella Succinogenes

scholarly journals Spectroscopic characterization of a high-potential monohaem cytochrome from Wolinella succinogenes, a nitrate-respiring organism. Redox and spin equilibria studies

1988 ◽  
Vol 177 (3) ◽  
pp. 673-682 ◽  
Author(s):  
Isabel MOURA ◽  
Ming Y. LIU ◽  
Cristina COSTA ◽  
Ming C. LIU ◽  
Govind PAI ◽  
...  
Keyword(s):  
Spectroscopic Characterization ◽  
High Potential ◽  
Wolinella Succinogenes

Regulation of anaerobic respiratory pathways in Wolinella succinogenes by the presence of electron acceptors

1993 ◽  
Vol 159 (5) ◽  
pp. 477-483 ◽  
Author(s):  
J. P. Lorenzen ◽  
A. Kr�ger ◽  
G. Unden
Keyword(s):  
Electron Acceptors ◽  
Wolinella Succinogenes

scholarly journals Cellulosomal Scaffoldin-Like Proteins fromRuminococcus flavefaciens

2001 ◽  
Vol 183 (6) ◽  
pp. 1945-1953 ◽  
Author(s):  
Shi-You Ding ◽  
Marco T. Rincon ◽  
Raphael Lamed ◽  
Jennifer C. Martin ◽  
Sheila I. McCrae ◽  
...  
Keyword(s):  
Direct Interaction ◽  
Rumen Bacterium ◽  
Type I ◽  
Gene Products ◽  
Type Ii ◽  
Direct Demonstration ◽  
Anchoring Protein ◽  
Domain Of Unknown Function ◽  
Signature Sequences ◽  
Related Proteins

ABSTRACT Two tandem cellulosome-associated genes were identified in the cellulolytic rumen bacterium, Ruminococcus flavefaciens. The deduced gene products represent multimodular scaffoldin-related proteins (termed ScaA and ScaB), both of which include several copies of explicit cellulosome signature sequences. The scaB gene was completely sequenced, and its upstream neighbor scaAwas partially sequenced. The sequenced portion of scaAcontains repeating cohesin modules and a C-terminal dockerin domain. ScaB contains seven relatively divergent cohesin modules, two extremely long T-rich linkers, and a C-terminal domain of unknown function. Collectively, the cohesins of ScaA and ScaB are phylogenetically distinct from the previously described type I and type II cohesins, and we propose that they define a new group, which we designated here type III cohesins. Selected modules from both genes were overexpressed inEscherichia coli, and the recombinant proteins were used as probes in affinity-blotting experiments. The results strongly indicate that ScaA serves as a cellulosomal scaffoldin-like protein for severalR. flavefaciens enzymes. The data are supported by the direct interaction of a recombinant ScaA cohesin with an expressed dockerin-containing enzyme construct from the same bacterium. The evidence also demonstrates that the ScaA dockerin binds to a specialized cohesin(s) on ScaB, suggesting that ScaB may act as an anchoring protein, linked either directly or indirectly to the bacterial cell surface. This study is the first direct demonstration in a cellulolytic rumen bacterium of a cellulosome system, mediated by distinctive cohesin-dockerin interactions.

scholarly journals Complete Genome Sequence of the Polysaccharide-Degrading Rumen Bacterium Pseudobutyrivibrio xylanivorans MA3014

2020 ◽  
Author(s):  
Nikola Palevich ◽  
Paul H. Maclean ◽  
William J. Kelly ◽  
Sinead C. Leahy ◽  
Jasna Rakonjac ◽  
...  
Keyword(s):  
Genome Sequence ◽  
Complete Genome Sequence ◽  
Complete Genome ◽  
Bacterial Species ◽  
Glycoside Hydrolases ◽  
Rumen Bacterium ◽  
Protein Coding ◽  
Plant Polysaccharides ◽  
Plant Matter ◽  
Genes Encoding

AbstractRuminants are essential for maintaining the global population and managing greenhouse gas emissions. In the rumen, bacterial species belonging to the genera rumen Butyrivibrio and Pseudobutyrivibrio constitute the core bacterial rumen microbiome and are important degraders of plant-derived complex polysaccharides. Pseudobutyrivibrio xylanivorans MA3014 was selected for genome sequencing in order to examine its ability to breakdown and utilize plant polysaccharides. The complete genome sequence of MA3014 is 3.58 Mb, consists of three replicons (a chromosome, chromid and plasmid), has an overall G+C content of 39.6% and encodes 3,265 putative protein-coding genes (PCGs). Comparative pan-genomics of all cultivated and currently available P. xylanivorans genomes has revealed highly open genomes and a strong correlation of orthologous genes within this species of rumen bacteria. MA3014 is metabolically versatile and capable of utilizing a range of simple mono-or oligosaccharides to complex plant polysaccharides such as pectins, mannans, starch and hemicelluloses for growth, with lactate, butyrate and formate as the principal fermentation end-products. The genes encoding these metabolic pathways have been identified and MA3014 is predicted to encode an extensive repertoire of Carbohydrate-Active enZYmes (CAZymes) with 80 Glycoside Hydrolases (GHs), 28 Carbohydrate Esterases (CEs) and 51 Glycosyl Transferases (GTs), that suggest its role as an initiator of primary solubilization of plant matter in the rumen.

The electrochemical proton potential generated by the sulphur respiration of Wolinella succinogenes

1989 ◽  
Vol 152 (6) ◽  
pp. 600-605 ◽  
Author(s):  
Christiane Wloczyk ◽  
Achim Kr�ger ◽  
Thomas G�bel ◽  
Gabriele Holdt ◽  
Ralf Steudel
Keyword(s):  
Wolinella Succinogenes ◽  
Proton Potential ◽  
Sulphur Respiration
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