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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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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, Jacques Mossé
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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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Dalton Trans., 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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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
W Mäntele
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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
W Mäntele
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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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Proceedings of the National Academy of Sciences of the United States of America, 2021
Jessica H Van Wonderen +2 more
exaly
Jessica H Van Wonderen +2 more
exaly
Structure function relationships within the multihemic cytochrome C3 superfamily
Journal of Inorganic Biochemistry, 1997M. Bruschi +3 more
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