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Directed evolution of copper nitrite reductase to a chromogenic reductant

Directed evolution of copper nitrite reductase to a chromogenic reductant

http://www.wikidata.org/entity/Q27659029

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Unique Heme-Iron Coordination by the Hemoglobin Receptor IsdB of Staphylococcus aureus Inactivation of the Heme Degrading Enzyme IsdI by an Active Site Substitution That Diminishes Heme Ruffling Characterization of a Nitrite Reductase Involved in Nitrifier Denitrification Biocatalyst development by directed evolution A Diatom Ferritin Optimized for Iron Oxidation but Not Iron Storage.SbnG, a citrate synthase in Staphylococcus aureus: a new fold on an old enzyme.Redox-coupled structural changes in nitrite reductase revealed by serial femtosecond and microfocus crystallography.IruO is a reductase for heme degradation by IsdI and IsdG proteins in Staphylococcus aureus.Structure-function analyses reveal key features in Staphylococcus aureus IsdB-associated unfolding of the heme-binding pocket of human hemoglobin.Potential for aerobic NO2- reduction and corresponding key enzyme genes involved in Alcaligenes faecalis strain NR.An unprecedented dioxygen species revealed by serial femtosecond rotation crystallography in copper nitrite reductase.New molecular packing in a crystal of pseudoazurin from Alcaligenes faecalis: a double-helical arrangement of blue copper.SbnI is a free serine kinase that generates O -phospho-l-serine for staphyloferrin B biosynthesis in Staphylococcus aureus.Engineering a bifunctional copper site in the cupredoxin fold by loop-directed mutagenesis

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Directed evolution of copper nitrite reductase to a chromogenic reductant

http://www.wikidata.org/entity/Q27659029

description

2010 nî lūn-bûn

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2010 թուականի Մարտին հրատարակուած գիտական յօդուած

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2010 թվականի մարտին հրատարակված գիտական հոդված

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2010年の論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年论文

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name

Directed evolution of copper nitrite reductase to a chromogenic reductant

@ast

Directed evolution of copper nitrite reductase to a chromogenic reductant

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Directed evolution of copper nitrite reductase to a chromogenic reductant

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type

label

Directed evolution of copper nitrite reductase to a chromogenic reductant

@ast

Directed evolution of copper nitrite reductase to a chromogenic reductant

@en

Directed evolution of copper nitrite reductase to a chromogenic reductant

@nl

prefLabel

Directed evolution of copper nitrite reductase to a chromogenic reductant

@ast

Directed evolution of copper nitrite reductase to a chromogenic reductant

@en

Directed evolution of copper nitrite reductase to a chromogenic reductant

@nl

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Protein Engineering Design and Selection

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Directed evolution of copper nitrite reductase to a chromogenic reductant

@en

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A Grant Mauk

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

Federico I Rosell

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

Iain S MacPherson

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

Melanie Scofield

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

P2860

The respiratory chains of Escherichia coli

Role of the axial ligand in type 1 Cu centers studied by point mutations of met148 in rusticyanin

Catalytic roles for two water bridged residues (Asp-98 and His-255) in the active site of copper-containing nitrite reductase

Alternate substrate binding modes to two mutant (D98N and H255N) forms of nitrite reductase from Alcaligenes faecalis S-6: structural model of a transient catalytic intermediate

Directing the mode of nitrite binding to a copper-containing nitrite reductase from Alcaligenes faecalis S-6: Characterization of an active site isoleucine

Reconstitution of the type-1 active site of the H145G/A variants of nitrite reductase by ligand insertion

The structure of copper-nitrite reductase from Achromobacter cycloclastes at five pH values, with NO2- bound and with type II copper depleted

Refinement of macromolecular structures by the maximum-likelihood method

Spectral and kinetic properties of the Fet3 protein from Saccharomyces cerevisiae, a multinuclear copper ferroxidase enzyme.

Mutagenicity studies of benzidine and its analogs: structure-activity relationships

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137-145

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10.1093/PROTEIN/GZP084

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3

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23

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41056124

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20083495

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directed evolution

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2816606

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