The tetraheme cytochrome from Shewanella oneidensis MR-1 shows thermodynamic bias for functional specificity of the hemes (Q45212040)

10 December 2017

The tetraheme cytochrome from Shewanella oneidensis MR-1 shows thermodynamic bias for functional specificity of the hemes (English)

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10 December 2017

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Shewanella oneidensis

Shewanella oneidensis

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6

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10 December 2017

Ivo H Saraiva

2

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Bruno M Fonseca

Bruno M Fonseca

1

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Catarina M Paquete

Catarina M Paquete

3

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Ricardo O Louro

Ricardo O Louro

7

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Cláudio M. Soares

Claudio M Soares

4

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author name string

Isabel Pacheco

5

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PubMed ID

19048308

10 December 2017

language of work or name

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2 December 2008

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Journal of Biological Inorganic Chemistry

10 December 2017

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10 December 2017

14

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10 December 2017

3

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10 December 2017

375-385

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https://scigraph.springernature.com/pub.10.1007/s00775-008-0455-7

10 December 2017

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Identification of 42 possible cytochrome C genes in the Shewanella oneidensis genome and characterization of six soluble cytochromes

21 January 2018

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Identification of a small tetraheme cytochrome c and a flavocytochrome c as two of the principal soluble cytochromes c in Shewanella oneidensis strain MR1

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Characterization of protein-protein interactions involved in iron reduction by Shewanella oneidensis MR-1.

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Current production and metal oxide reduction by Shewanella oneidensis MR-1 wild type and mutants

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Identification and characterization of a novel cytochrome c(3) from Shewanella frigidimarina that is involved in Fe(III) respiration

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Crystal structures at atomic resolution reveal the novel concept of "electron-harvesting" as a role for the small tetraheme cytochrome c

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A directional electron transfer regulator based on heme-chain architecture in the small tetraheme cytochrome c from Shewanella oneidensis.

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Electrochemical interrogations of the Mtr cytochromes from Shewanella: opening a potential window

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NMR structure of the haem core of a novel tetrahaem cytochrome isolated from Shewanella frigidimarina: identification of the haem-specific axial ligands and order of oxidation

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Electron transfers in chemistry and biology

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Proton thrusters: overview of the structural and functional features of soluble tetrahaem cytochromes c3.

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Proton-assisted two-electron transfer in natural variants of tetraheme cytochromes from Desulfomicrobium Sp.

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Studies of the reduction and protonation behavior of tetraheme cytochromes using atomic detail

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Electrostatic calculations of the pKa values of ionizable groups in bacteriorhodopsin

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Reorganization and conformational changes in the reduction of tetraheme cytochromes

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NMR studies of electron transfer mechanisms in a protein with interacting redox centres: Desulfovibrio gigas cytochrome c3.

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Thermodynamic characterization of a tetrahaem cytochrome isolated from a facultative aerobic bacterium, Shewanella frigidimarina: a putative redox model for flavocytochrome c3.

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The protein moiety modulates the redox potential in cytochromes c.

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Structure and mechanism of the flavocytochrome c fumarate reductase of Shewanella putrefaciens MR-1

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Natural engineering principles of electron tunnelling in biological oxidation-reduction

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Differential influence of dynamic processes on forward and reverse electron transfer across a protein-protein interface

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Electron tunneling through proteins

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Convergence Properties of the Nelder--Mead Simplex Method in Low Dimensions

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The GROMOS Biomolecular Simulation Program Package

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On the use of different dielectric constants for computing individual and pairwise terms in poisson-boltzmann studies of protein ionization equilibrium

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Distance dependence of interactions between charged centres in proteins with common structural features

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Assignment of the redox potentials to the four haems in Desulfovibrio vulgaris cytochrome c 3 by 2D-NMR

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Determination of the orientation of the axial ligands and of the magnetic properties of the haems in the tetrahaem ferricytochrome from Shewanella frigidimarina

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12 December 2020

Identification of residues contributing to the Bohr effect of human haemoglobin

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12 December 2020

Localization and specificity of cytochromes and other electron transfer proteins from sulfate-reducing bacteria

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12 December 2020

NMR studies of cooperativity in the tetrahaem cytochrome c3 from Desulfovibrio vulgaris

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12 December 2020

Thermodynamic and kinetic characterisation of individual haems in multicentre cytochromes c3

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12 December 2020

Cooperativity between electrons and protons in a monomeric cytochrome c(3): the importance of mechano-chemical coupling for energy transduction

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12 December 2020

Determination of haem electronic structure in His-Met cytochromes c by 13C-NMR. The effect of the axial ligands

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12 December 2020

Binding of ligands originates small perturbations on the microscopic thermodynamic properties of a multicentre redox protein

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12 December 2020

10.1007/S00775-008-0455-7

Identifiers

DOI

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PubMed ID

19048308

Dimensions Publication ID

10 December 2017

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1 reference

PubMed ID

19048308