SERR Spectroelectrochemical Study of Cytochrome cd1 Nitrite Reductase Co-Immobilized with Physiological Redox Partner Cytochrome c552 on Biocompatible Metal Electrodes.

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Synchrotron-Based Infrared Microanalysis of Biological Redox Processes under Electrochemical Control Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase.Structure, electrocatalysis and dynamics of immobilized cytochrome PccH and its microperoxidase.

P2860

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P2860

SERR Spectroelectrochemical Study of Cytochrome cd1 Nitrite Reductase Co-Immobilized with Physiological Redox Partner Cytochrome c552 on Biocompatible Metal Electrodes.

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http://www.wikidata.org/entity/Q35668764

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2015 nî lūn-bûn

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2015年の論文

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2015年論文

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2015年論文

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2015年論文

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2015年論文

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2015年論文

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2015年论文

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2015年论文

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2015年论文

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name

SERR Spectroelectrochemical St ...... iocompatible Metal Electrodes.

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SERR Spectroelectrochemical St ...... iocompatible Metal Electrodes.

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Item

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SERR Spectroelectrochemical St ...... iocompatible Metal Electrodes.

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SERR Spectroelectrochemical St ...... iocompatible Metal Electrodes.

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SERR Spectroelectrochemical St ...... iocompatible Metal Electrodes.

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SERR Spectroelectrochemical St ...... iocompatible Metal Electrodes.

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P1476

SERR Spectroelectrochemical St ...... iocompatible Metal Electrodes.

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P2093

José J G Moura

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M Gabriela Almeida

http://www.w3.org/2001/XMLSchema#string

Pedro O Quintas

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P2860

Analyzing the catalytic processes of immobilized redox enzymes by vibrational spectroscopies

Does the reduction of c heme trigger the conformational change of crystalline nitrite reductase?

MAD structure of Pseudomonas nautica dimeric cytochrome c552 mimicks the c4 Dihemic cytochrome domain association

Structure of the open conformation of a functional chimeric NADPH cytochrome P450 reductase

Haem-ligand switching during catalysis in crystals of a nitrogen-cycle enzyme

N-terminal arm exchange is observed in the 2.15 A crystal structure of oxidized nitrite reductase from Pseudomonas aeruginosa

Conformational changes occurring upon reduction and NO binding in nitrite reductase from Pseudomonas aeruginosa

Investigations of heme distortion, low-frequency vibrational excitations, and electron transfer in cytochrome c

Intramolecular electron transfer in nitrite reductases.

Electrical contacting of redox proteins by nanotechnological means.

P304

e0129940

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scholarly article

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10.1371/JOURNAL.PONE.0129940

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English

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2015-06-19T00:00:00Z

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26091174

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4474632

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SERR Spectroelectrochemical Study of Cytochrome cd1 Nitrite Reductase Co-Immobilized with Physiological Redox Partner Cytochrome c552 on Biocompatible Metal Electrodes.

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P2860

P2860

SERR Spectroelectrochemical Study of Cytochrome cd1 Nitrite Reductase Co-Immobilized with Physiological Redox Partner Cytochrome c552 on Biocompatible Metal Electrodes.

description

name

type

label

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P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

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P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

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P698

P932