Scanning Electrochemical Microscopy of Cytochrome c Peroxidase through the Orientation‐Controlled Immobilisation of Cytochrome c
نویسندگان
چکیده
منابع مشابه
The crystal structure of cytochrome c peroxidase.
The three-dimensional conformation of yeast cytochrome c peroxidase has been determined from a 2.5 A electron density map computed with phases obtained from two isomorphous mercury derivatives. Partial sequence information that has recently become available aided in completion of the tracing of the polypeptide backbone, confirmed the presence of a proximal histidine heme ligand and aided in ide...
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Apoproteins of cytochrome c peroxidase, horseradish peroxidase, and sperm whale myoglobin were recombined with manganese complexes of proto-, hemato-, meso-, and deuteroporphyrins to form manganese porphyrin-protein complexes. These complexes were purified by column chromatography. All the manganese porphyrin-containing cytochrome c peroxidases were crystallized. Light absorption maxima of mang...
متن کاملInvestigation of electron tunneling between cytochrome c peroxidase and cytochrome c.
The nature of electron transfer between the bound complex cytochrome c and cytochrome c peroxidase has been investigated. Experimental verification of the predicted charge-transfer band provides evidence of electron tunneling as the mechanism of transfer between these molecules in solution at room temperature. The measured transfer distance is congruent to 7 angstroms between heme edges, which ...
متن کاملIn-silico Assessment of Protein-Protein Electron Transfer. A Case Study: Cytochrome c Peroxidase – Cytochrome c
The fast development of software and hardware is notably helping in closing the gap between macroscopic and microscopic data. Using a novel theoretical strategy combining molecular dynamics simulations, conformational clustering, ab-initio quantum mechanics and electronic coupling calculations, we show how computational methodologies are mature enough to provide accurate atomistic details into ...
متن کاملCrystal structure and characterization of a cytochrome c peroxidase-cytochrome c site-specific cross-link.
A specific covalently cross-linked complex between redox partners yeast cytochrome c peroxidase (CCP) and cytochrome c (cyt. c) has been made by engineering cysteines into CCP and cyt. c that form an intermolecular disulfide bond in high yield. The crystal structure of the cross-linked complex has been solved to 1.88-A resolution and closely resembles the structure of the noncovalent complex [P...
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ژورنال
عنوان ژورنال: ChemElectroChem
سال: 2016
ISSN: 2196-0216,2196-0216
DOI: 10.1002/celc.201600195