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Tools for resolving complexity in the electron transfer networks of multiheme cytochromes c
Metallomics, 2011Examining electron transfer between two proteins with identical spectroscopic signatures is a challenging task. It is supposed that several multiheme cytochromes in Shewanella oneidensis form a molecular "wire" through which electrons are transported across the cellular space and a direct study of this transient protein-protein interaction has not yet ...
Mackenzie A, Firer-Sherwood +3 more
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Heme Cluster Structures and Electron Transfer in Multiheme Cytochromes C3
1987Cytochromes C3 (molecular weight around 14000) form a class of multiheme cytochromes which are present in all anaerobic sulfate-reducing bacteria belonging to the genus Desulfovibrio (1). They are essential electron carriers in several electron transfer processes and their oxidation-reduction properties have been studied in some detail (2).
Richard Haser
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Redox-linked conformational changes of a multiheme cytochrome from Geobacter sulfurreducens
Biochemical and Biophysical Research Communications, 2007Multiheme c-type cytochromes from members of the Desulfovibrionacea and Geobactereacea families play crucial roles in the bioenergetics of these microorganisms. Thermodynamic studies using NMR and visible spectroscopic techniques on tetraheme cytochromes c(3) isolated from Desulfovibrio spp.
Morgado, Leonardo +5 more
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Dalton Transactions, 2010
Shewanella are facultative anaerobic bacteria of remarkable respiratory versatility that includes the dissimilatory reduction of metal ores. They contain a large number of multiheme c-type cytochromes that play a significant role in various anaerobic respiratory processes.
Catarina M Paquete, Ricardo O Louro
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Shewanella are facultative anaerobic bacteria of remarkable respiratory versatility that includes the dissimilatory reduction of metal ores. They contain a large number of multiheme c-type cytochromes that play a significant role in various anaerobic respiratory processes.
Catarina M Paquete, Ricardo O Louro
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Isotopic labeling of c-type multiheme cytochromes overexpressed in E. coli
Protein Expression and Purification, 2008Progresses made in bacterial genome sequencing show a remarkable profusion of multiheme c-type cytochromes in many bacteria, highlighting the importance of these proteins in different cellular events. However, the characterization of multiheme cytochromes has been significantly retarded by the numerous experimental challenges encountered by researchers
Ana P, Fernandes +4 more
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Conformational properties of multihemic cytochromes c from Desulfuromonas acetoxidans
Thermochimica Acta, 2003Abstract In the classification of c-type cytochromes, the class III includes multihemic cytochromes c with low redox potential constituting the cytochrome c3 superfamily. Most of the cytochromes described have been isolated from sulfate or sulfur reducing bacteria.
M.T. Giudici-Orticoni +5 more
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Possible Dynamically Gated Conductance along Heme Wires in Bacterial Multiheme Cytochromes
The Journal of Physical Chemistry B, 2014The staggered cross decaheme configuration of electron transfer cofactors in the outer-membrane cytochrome MtrF serves as a prototype for conformationally gated multiheme electron transport. Derived from the bacterium Shewanella oneidensis, the staggered cross configuration reveals intersecting c-type octaheme and tetraheme "wires" containing ...
Dayle M A, Smith, Kevin M, Rosso
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Electron transfer between hydrogenases and mono- and multiheme cytochromes in Desulfovibrio ssp
JBIC Journal of Biological Inorganic Chemistry, 1998A comparative study of electron transfer between the 16 heme high molecular mass cytochrome (Hmc) from Desulfovibrio vulgaris Hildenborough and the [Fe] and [NiFe] hydrogenases from the same organism was carried out, both in the presence and in the absence of catalytic amounts of cytochrome c3.
Inês A. C. Pereira +4 more
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1993
The photosynthetic reaction center (RC) of Cf. aurantiacus contains a multiheme cytochrome subunit which is responsible for the rereduction of the photooxidized primary electron donor. In contrast to the hemes of the cytochrome subunit of Rps.vihdis, all hemes exhibit the same α-band absorption at 554 nm, thus rendering an individual titration of their
F. Fritz +3 more
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The photosynthetic reaction center (RC) of Cf. aurantiacus contains a multiheme cytochrome subunit which is responsible for the rereduction of the photooxidized primary electron donor. In contrast to the hemes of the cytochrome subunit of Rps.vihdis, all hemes exhibit the same α-band absorption at 554 nm, thus rendering an individual titration of their
F. Fritz +3 more
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Photoexcited flavins and pterins as electron injectors for multiheme cytochrome
Doklady Biochemistry and Biophysics, 2009M S, Kritsky +5 more
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