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 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 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

scholarly journals Separate binding sites for antimycin and mucidin in the respiratory chain of the bacterium Paracoccus denitrificans and their occurrence in other denitrificans bacteria

1988 ◽  
Vol 252 (3) ◽  
pp. 905-908 ◽  
Author(s):  
I Kucera ◽  
R Hedbávný ◽  
V Dadák
Keyword(s):  
Respiratory Chain ◽  
Binding Sites ◽  
Paracoccus Denitrificans ◽  
Pseudomonas Stutzeri ◽  
Bc1 Complex ◽  
Cytochrome Bc1 Complex ◽  
Q Cycle ◽  
Cytochromes C ◽  
Fluorimetric Titration

By means of the method of fluorimetric titration it has been shown that mucidin does not affect the attachment of antimycin to membranes from anaerobically grown Paracoccus denitrificans. The fluorimetric titration with antimycin can be used in the determination of the amount of the cytochrome bc1 complex in the membrane. In cells inhibited with antimycin, the oxidation of cytochromes c was accompanied by the reduction of cytochrome b; in the presence of mucidin this effect did not take place. The results, which indicated a difference in binding sites, were interpreted in terms of the Q-cycle [Mitchell (1976) J. Theor. Biol. 62, 327-367; Trumpower (1981) Biochim. Biophys. Acta 639, 129-155]. Comparable sensitivity towards antimycin and mucidin was shown by other typical denitrifying bacteria: Pseudomonas stutzeri and Alcaligenes xylosoidans, subspecies denitrificans.

High- and low-affinity binding sites for Cd on the bacterial cell walls of Bacillus subtilis and Shewanella oneidensis

2010 ◽  
Vol 74 (15) ◽  
pp. 4219-4233 ◽  
Author(s):  
Bhoopesh Mishra ◽  
Maxim Boyanov ◽  
Bruce A. Bunker ◽  
Shelly D. Kelly ◽  
Kenneth M. Kemner ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Binding Sites ◽  
Bacterial Cell ◽  
Cell Walls ◽  
Shewanella Oneidensis ◽  
Affinity Binding ◽  
Bacterial Cell Walls

Evidence for binding sites on cytochrome c for oxidases and reductases from studies of different cytochromes c of known structure

Biochemistry ◽  
1976 ◽  
Vol 15 (26) ◽  
pp. 5827-5831 ◽  
Author(s):  
Lucile Smith ◽  
Helen C. Davies ◽  
Maria E. Nava
Keyword(s):  
Cytochrome C ◽  
Binding Sites ◽  
Cytochromes C

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.

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