The Crystal Structure of the Extracellular 11-heme Cytochrome UndA Reveals a Conserved 10-heme Motif and Defined Binding Site for Soluble Iron Chelates [PDF]
Members of the genus Shewanella translocate deca- or undeca-heme cytochromes to the external cell surface thus enabling respiration using extracellular minerals and polynuclear Fe(III) chelates.
Butt, Julea N.+7 more
core +2 more sources
The crystal structure of a biological insulated transmembrane molecular wire [PDF]
A growing number of bacteria are recognized to conduct electrons across their cell envelope, and yet molecular details of the mechanisms supporting this process remain unknown.
Butt, Julea+4 more
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Structure-Guided Recombination Creates an Artificial Family of Cytochromes P450 [PDF]
Creating artificial protein families affords new opportunities to explore the determinants of structure and biological function free from many of the constraints of natural selection.
Arnold, Frances H.+5 more
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Redox linked flavin sites in extracellular decaheme proteins involved in microbe-mineral electron transfer [PDF]
Extracellular microbe-mineral electron transfer is a major driving force for the oxidation of organic carbon in many subsurface environments. Extracellular multi-heme cytochromes of the Shewenella genus play a major role in this process but the mechanism
A Okamoto+35 more
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Structure of a bacterial cell surface decaheme electron conduit [PDF]
Some bacterial species are able to utilize extracellular mineral forms of iron and manganese as respiratory electron acceptors. In Shewanella oneidensis this involves decaheme cytochromes that are located on the bacterial cell surface at the termini of ...
A. Hall+34 more
core +3 more sources
Cytochrome P450associated with insecticide resistance catalyzes cuticular hydrocarbon production in Anopheles gambiae. [PDF]
The role of cuticle changes in insecticide resistance in the major malaria vector Anopheles gambiae was assessed. The rate of internalization of 14C deltamethrin was significantly slower in a resistant strain than in a susceptible strain.
Anthousi, Amalia+14 more
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The interactions of cytochrome c and porphyrin cytochrome c with cytochrome c oxidase. The resting, reduced and pulsed enzymes [PDF]
Cytochrome c oxidase forms tight binding complexes with the cytochrome c analog, porphyrin cytochrome c. The behaviour of the reduced and pulsed forms of the oxidase with porphyrin cytochrome c have been followed as functions of ionic strength; this behaviour has been compared with that of the resting oxidase [Kornblatt, Hui Bon Hoa and English (1984 ...
Hue Anh Luu, Jack A. Kornblatt
openaire +3 more sources
Amino acid sequence, haem-iron co-ordination geometry and functional properties of mitochondrial and bacterial c-type cytochromes [PDF]
Cytochromes are found in all biological oxidation Systems which involve transport of reducing equivalents through organized chains of membrane bound intermediates, regardless of the ultimate oxidant (Keilin, 1966; Bartsch, 1978; Meyer & Kamen, 1982 ...
Senn, Hans, Wüthrich, Kurt
core
H NMR Studies of Eukaryotic Cytochrome c [PDF]
H NMR resonance assignments in the spectra of horse, tuna, Neurmpora crassa and Candida krusei cyto-chromes c are described. Assignments have been made using NMR double-resonance techniques in conjunction with electron-exchange experiments, spectral ...
Boswell+17 more
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Cytochrome c signalosome in mitochondria [PDF]
Cytochrome c delicately tilts the balance between cell life (respiration) and cell death (apoptosis). Whereas cell life is governed by transient electron transfer interactions of cytochrome c inside the mitochondria, the cytoplasmic adducts of cytochrome c that lead to cell death are amazingly stable.
Díaz Moreno, Irene+3 more
openaire +5 more sources