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Chemicals, plastics and rubber industries

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Electron transfer and electrocatalytic properties of the immobilized methionine80alanine cytochrome c variant

Article Abstract:

The studies of the redox properties of M80A, a variant of yeast iso-1-cytochrome c (cytc) chemisorbed on a solid (gold) electrode coated with negatively charged 4-mercaptopyridine or carboxylalkanethiol self-assembled monolayers (SAM) is presented. The M80A cytc, as a suitable constituent of a biocatalytic interface for oxygen biosensing could be used to engineer cytochrome c in the bio-based detection of chemicals of environmental and clinical interest.

Author: Battistuzzi, Gianantonio, Borsari, Marco, Bortolotti, Carlo Augusto, Ranieri, Antonio, Sola, Marco, Casalini, Stefano
Publisher: American Chemical Society
Publication Name: Journal of Physical Chemistry B
Subject: Chemicals, plastics and rubber industries
ISSN: 1520-6106
Year: 2008
Science & research, Research, Oxidation-reduction reactions, Electron transport, Alanine

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The coupling of protonation and reduction in proteins with multiple redox centers: theory, computational method, and application to cytochrome c3

Article Abstract:

The coupling of protonation and reduction is crucial in many biological charge transfer reactions and is known as redox Bohr effect and it is caused by electrostatic interactions between protonatable and redox-active groups. The study discusses the energetic of protonation and redox reactions throughout the whole investigated pH and solution redox potential range.

Author: Ullmann, G. Mattthias
Publisher: American Chemical Society
Publication Name: Journal of Physical Chemistry B
Subject: Chemicals, plastics and rubber industries
ISSN: 1520-6106
Year: 2000
Proteins, Oxidation reduction reactions

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Protonation of the proximal histidine ligand in heme peroxidases

Article Abstract:

The protonation status of the Fe-His-Asp motif in all reaction intermediates for cytochrome c peroxidase is examined. Combined quantum and molecular mechanics (QM/MM) calculations have shown that the proton has preferred to reside on the His ligand in all states in the reaction mechanism of the peroxidases.

Author: Ryde, Ulf, Rydberg, Patrik, Heimdal, Jimmy
Publisher: American Chemical Society
Publication Name: Journal of Physical Chemistry B
Subject: Chemicals, plastics and rubber industries
ISSN: 1520-6106
Year: 2008
Quantum theory, Quantum mechanics, Peroxidase

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Subjects list: Analysis, Oxidation-reduction reaction, Cytochrome c, Chemical properties
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