scholarly journals Evidence for quinol oxidase activity of ImoA, a novel NapC/NirT family protein from the neutrophilic Fe(II) oxidizing bacterium Sideroxydans lithotrophicus ES-1

2022 ◽  
Author(s):  
Abhiney Jain ◽  
Anaísa Coelho ◽  
Joana Madjarov ◽  
Smilja Todorovic ◽  
Ricardo O. Louro ◽  
...  
Keyword(s):  
Electron Flow ◽  
Shewanella Oneidensis ◽  
Anaerobic Respiration ◽  
Plasmid Vector ◽  
Spectroscopic Characterization ◽  
Quinone Reductase ◽  
Inner Membrane ◽  
Quinol Oxidase ◽  
Wide Range ◽  
Tetraheme Cytochrome

The freshwater chemolithoautotrophic Gram-negative bacterium Sideroxydans lithotrophicus ES-1 oxidizes Fe(II) at the cell surface. In this organism, it is proposed that the monoheme cytochrome MtoD from the Mto pathway transfer electrons across the periplasm to an inner membrane NapC/NirT family tetraheme cytochrome encoded by Slit_2495, for which we propose the name ImoA (inner membrane oxidoreductase). ImoA has been proposed to function as the quinone reductase, receiving electrons from iron oxidizing extracellular electron uptake pathway to reduce the quinone pool. In this study, ImoA was cloned on a pBAD plasmid vector and overexpressed in Escherichia coli. Biochemical and spectroscopic characterization of the purified ImoA reveals that this 26.5 kDa cytochrome contains one high-spin and three low-spin hemes. Our data show that ImoA can function as a quinol oxidase and is able to functionally replace CymA, a related NapC/NirT family tetraheme cytochrome required for anaerobic respiration of a wide range of substrates by Shewanella oneidensis. We demonstrate that ImoA can transfer electrons to different periplasmic proteins from S. oneidensis including STC and FccA, but in a manner that is distinct from that of CymA. Phylogenetic analysis shows that ImoA is clustered closer to NirT sequences than to CymA. This study suggests that ImoA functions as a quinol oxidase in S. oneidensis and raises questions about the directionality and/or reversibility of electron flow through the Mto pathway in S. lithotrophicus ES-1.

scholarly journals Identification of a Small Tetraheme Cytochromec and a Flavocytochrome c as Two of the Principal Soluble Cytochromes c inShewanella oneidensis Strain MR1

2001 ◽  
Vol 67 (7) ◽  
pp. 3236-3244 ◽  
Author(s):  
A. I. Tsapin ◽  
I. Vandenberghe ◽  
K. H. Nealson ◽  
J. H. Scott ◽  
T. E. Meyer ◽  
...  
Keyword(s):  
Binding Sites ◽  
Shewanella Oneidensis ◽  
Structural Comparison ◽  
Facultative Anaerobe ◽  
Shewanella Frigidimarina ◽  
Cytochromes C ◽  
Flavocytochrome C ◽  
Tetraheme Cytochrome ◽  
Small Tetraheme Cytochrome ◽  
Genetic Context

ABSTRACT Two abundant, low-redox-potential cytochromesc were purified from the facultative anaerobeShewanella oneidensis strain MR1 grown anaerobically with fumarate. The small cytochrome was completely sequenced, and the genes coding for both proteins were cloned and sequenced. The small cytochrome c contains 91 residues and four heme binding sites. It is most similar to the cytochromes c fromShewanella frigidimarina (formerly Shewanella putrefaciens) NCIMB400 and the unclassified bacterial strain H1R (64 and 55% identity, respectively). The amount of the small tetraheme cytochrome is regulated by anaerobiosis, but not by fumarate. The larger of the two low-potential cytochromes contains tetraheme and flavin domains and is regulated by anaerobiosis and by fumarate and thus most nearly corresponds to the flavocytochromec-fumarate reductase previously characterized fromS. frigidimarina to which it is 59% identical. However, the genetic context of the cytochrome genes is not the same for the twoShewanella species, and they are not located in multicistronic operons. The small cytochrome c and the cytochrome domain of the flavocytochrome c are also homologous, showing 34% identity. Structural comparison shows that theShewanella tetraheme cytochromes are not related to theDesulfovibrio cytochromes c 3but define a new folding motif for small multiheme cytochromesc.

scholarly journals Erratum to: The tetraheme cytochrome from Shewanella oneidensis MR-1 shows thermodynamic bias for functional specificity of the hemes

2011 ◽  
Vol 16 (2) ◽  
pp. 357-358
Author(s):  
Bruno M. Fonseca ◽  
Ivo H. Saraiva ◽  
Catarina M. Paquete ◽  
Claudio M. Soares ◽  
Isabel Pacheco ◽  
...  
Keyword(s):  
Shewanella Oneidensis ◽  
Functional Specificity ◽  
Tetraheme Cytochrome

Effect of NAD+-dependent formate dehydrogenase on anaerobic respiration of Shewanella oneidensis MR-1

Microbiology ◽  
2013 ◽  
Vol 82 (4) ◽  
pp. 404-409 ◽  
Author(s):  
N. N. Mordkovich ◽  
T. A. Voeikova ◽  
L. M. Novikova ◽  
I. A. Smirnov ◽  
V. K. Il’in ◽  
...  
Keyword(s):  
Formate Dehydrogenase ◽  
Shewanella Oneidensis ◽  
Anaerobic Respiration

Effects of sulfate concentration and sludge retention time on the interaction between methane production and sulfate reduction for butyrate

1994 ◽  
Vol 30 (8) ◽  
pp. 45-54 ◽  
Author(s):  
O. Mizuno ◽  
Y. Y. Li ◽  
T. Noike
Keyword(s):  
Sulfate Reduction ◽  
Retention Time ◽  
Methane Production ◽  
Electron Flow ◽  
Degradation Pathway ◽  
Sulfate Concentration ◽  
High Concentration ◽  
Total Electron ◽  
Sludge Retention Time ◽  
Wide Range

The effects of sulfate concentration and COD/S ratio on the anaerobic degradation of butyrate were investigated by using 2.0 L anaerobic chemostat-type reactor at 35°C. The study was conducted over a wide range of the COD/S ratio (1.5 to 148) by varying COD concentrations (2500–10000 mg/L) and sulfate concentrations (68–1667 mg-S/L) in the substrate. The sludge retention time at each COD/S ratio was changed from 5 to 20 days. The interaction between methane producing bacteria (MPB) and sulfate-reducing bacteria (SRB) was evidently influenced by COD/S ratio in the substrate. When COD/S ratio was 6.0 or more, methane production was the predominate reaction and over 80% of the total electron flow was used by MPB. At the COD/S ratio of 1.5, SRB utilzed over 50% of the total electron flow. A large amount of sulfate reduction resulted in not only the decrease of methane production, but also the rapid increase of the bacterial growth. The degradation pathway of butyrate and the composition of bacterial populations in the reactor were also dominated by COD/S ratio. In sulfate depleted condition, butyrate was degraded to methane via acetate and hydrogen by MPB. On the other hand, butyrate was firstly degraded into sulfide and acetate in sulfate rich conditions by SRB, and the produced acetate was then degraded by acetate consuming MPB and SRB. The methanogenesis from acetate was inhibited by the high concentration of sulfide.

scholarly journals Electron Flow between Photosystem II and Oxygen in Chloroplasts of Photosystem I-deficient Algae Is Mediated by a Quinol Oxidase Involved in Chlororespiration

2000 ◽  
Vol 275 (23) ◽  
pp. 17256-17262 ◽  
Author(s):  
Laurent Cournac ◽  
Kevin Redding ◽  
Jacques Ravenel ◽  
Dominique Rumeau ◽  
Eve-Marie Josse ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Photosystem I ◽  
Electron Flow ◽  
Quinol Oxidase

scholarly journals A Hybrid Extracellular Electron Transfer Pathway Enhances the Survival of Vibrio natriegens

2020 ◽  
Vol 86 (19) ◽  
Author(s):  
Bridget E. Conley ◽  
Matthew T. Weinstock ◽  
Daniel R. Bond ◽  
Jeffrey A. Gralnick
Keyword(s):  
Electron Transfer ◽  
Shewanella Oneidensis ◽  
Anaerobic Respiration ◽  
Basic Research ◽  
Extracellular Electron Transfer ◽  
Content Type ◽  
Electron Transfer Pathway ◽  
Sedimentary Environments ◽  
Genetic Potential ◽  
Iron And Manganese

ABSTRACT Vibrio natriegens is the fastest-growing microorganism discovered to date, making it a useful model for biotechnology and basic research. While it is recognized for its rapid aerobic metabolism, less is known about anaerobic adaptations in V. natriegens or how the organism survives when oxygen is limited. Here, we describe and characterize extracellular electron transfer (EET) in V. natriegens, a metabolism that requires movement of electrons across protective cellular barriers to reach the extracellular space. V. natriegens performs extracellular electron transfer under fermentative conditions with gluconate, glucosamine, and pyruvate. We characterized a pathway in V. natriegens that requires CymA, PdsA, and MtrCAB for Fe(III) citrate and Fe(III) oxide reduction, which represents a hybrid of strategies previously discovered in Shewanella and Aeromonas. Expression of these V. natriegens genes functionally complemented Shewanella oneidensis mutants. Phylogenetic analysis of the inner membrane quinol dehydrogenases CymA and NapC in gammaproteobacteria suggests that CymA from Shewanella diverged from Vibrionaceae CymA and NapC. Analysis of sequenced Vibrionaceae revealed that the genetic potential to perform EET is conserved in some members of the Harveyi and Vulnificus clades but is more variable in other clades. We provide evidence that EET enhances anaerobic survival of V. natriegens, which may be the primary physiological function for EET in Vibrionaceae. IMPORTANCE Bacteria from the genus Vibrio occupy a variety of marine and brackish niches with fluctuating nutrient and energy sources. When oxygen is limited, fermentation or alternative respiration pathways must be used to conserve energy. In sedimentary environments, insoluble oxide minerals (primarily iron and manganese) are able to serve as electron acceptors for anaerobic respiration by microorganisms capable of extracellular electron transfer, a metabolism that enables the use of these insoluble substrates. Here, we identify the mechanism for extracellular electron transfer in Vibrio natriegens, which uses a combination of strategies previously identified in Shewanella and Aeromonas. We show that extracellular electron transfer enhanced survival of V. natriegens under fermentative conditions, which may be a generalized strategy among Vibrio spp. predicted to have this metabolism.

scholarly journals A directional electron transfer regulator based on heme-chain architecture in the small tetraheme cytochrome c from Shewanella oneidensis

FEBS Letters ◽  
2002 ◽  
Vol 532 (3) ◽  
pp. 333-337 ◽  
Author(s):  
Erisa Harada ◽  
Jiro Kumagai ◽  
Kiyoshi Ozawa ◽  
Shinichiro Imabayashi ◽  
Alexandre S Tsapin ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Cytochrome C ◽  
Shewanella Oneidensis ◽  
Chain Architecture ◽  
Tetraheme Cytochrome ◽  
Small Tetraheme Cytochrome

scholarly journals Kinetic stability properties of relativistic nonneutral electron flow for low-frequency extraordinary-mode perturbations

1989 ◽  
Vol 7 (1) ◽  
pp. 85-109 ◽  
Author(s):  
Ronald C. Davidson ◽  
Han S. Uhm
Keyword(s):  
Dispersion Relation ◽  
Layer Thickness ◽  
Electron Energy ◽  
Electron Flow ◽  
Low Frequency ◽  
Outer Edge ◽  
Stability Properties ◽  
System Parameters ◽  
Wide Range ◽  
Electron Layer

The kinetic stability properties of relativistic nonneutral electron flow in planar diode geometry are examined for extraordinary-mode perturbations about the self-consistent Vlasov equilibrium . Here, the cathode is located at x = 0; the anode is located at x = d the outer edge of the electron layer is located at is the equilibrium flow velocity in the x-direction; n^b is the electron density at the cathode (x = 0); and is the axial magnetic field, with const. in the vacuum region (xb < x ≤ d). The extraordinary-mode eigenvalue equation, derived in a companion paper for low-frequency, long-wavelength perturbations, is solved exactly. This leads to a formal dispersion relation, which can be used to determine the complex eigenfrequency ω over a wide range of system parameters and wavenumber k in the y-direction. The formal dispersion relation is further simplified for and , assuming low-frequency perturbations about a tenuous electron layer with and . Here, , and , where denotes the average equilibrium orbit, and [γ(x) − 1]mc2 is the average kinematic energy of an electron fluid element. The resulting approximate dispersion relation is solved numerically over a wide range of system parameters to determine the detailed dependence of stability properties on electromagnetic effects, layer thickness, and electron energy, as measured by , and γb − 1, respectively. Here, γb = γ(xb) denotes the electron energy at the outer edge of the electron layer. As a general remark, it is found that increasing the electron energy (γb − 1), increasing the strength of electromagnetic effects , and/or decreasing the layer thickness (xb/d) all have a stabilizing influence.

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