Results 141 to 150 of about 885 (161)
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Possible Dynamically Gated Conductance along Heme Wires in Bacterial Multiheme Cytochromes

The Journal of Physical Chemistry B, 2014
The 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
openaire   +2 more sources

Heme Cluster Structures and Electron Transfer in Multiheme Cytochromes C3

1987
Cytochromes 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
openaire   +1 more source

Electron transfer between hydrogenases and mono- and multiheme cytochromes in Desulfovibrio ssp

JBIC Journal of Biological Inorganic Chemistry, 1998
A 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
openaire   +1 more source

Molecular details of multielectron transfer: the case of multiheme cytochromes from metal respiring organisms

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
openaire   +2 more sources

Electrochemical and Spectroscopical Characterisation of the Multiheme Cytochrome Subunit of the Reaction Center of Chloroflexus Aurantiacus

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
exaly   +2 more sources

Multiheme Cytochromes

2016
Carlos A. Salgueiro, Joana M. Dantas
openaire   +2 more sources

Photoexcited flavins and pterins as electron injectors for multiheme cytochrome

Doklady Biochemistry and Biophysics, 2009
M S, Kritsky   +5 more
openaire   +2 more sources

Nanosecond heme-to-heme electron transfer rates in a multiheme cytochrome nanowire reported by a spectrally unique His/Met-ligated heme

Proceedings of the National Academy of Sciences of the United States of America, 2021
Jessica H Van Wonderen   +2 more
exaly  

Structure function relationships within the multihemic cytochrome C3 superfamily

Journal of Inorganic Biochemistry, 1997
M. Bruschi   +3 more
openaire   +1 more source

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