15N-NMR characterization of His residues in and around the active site of FeSOD.

about

Superoxide dismutases and superoxide reductases.Superoxide dismutases: ancient enzymes and new insights.Engineering a dirhodium artificial metalloenzyme for selective olefin cyclopropanation.Combined QM/MM and Monte Carlo study for redox leveling in Mn and Fe superoxide dismutase.

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P2860

15N-NMR characterization of His residues in and around the active site of FeSOD.

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http://www.wikidata.org/entity/Q43237310

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2009 nî lūn-bûn

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2009年の論文

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2009年学术文章

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2009年学术文章

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2009年学术文章

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2009年学术文章

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2009年学术文章

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2009年学术文章

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2009年學術文章

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2009年學術文章

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name

15N-NMR characterization of His residues in and around the active site of FeSOD.

@en

15N-NMR characterization of His residues in and around the active site of FeSOD.

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type

Item

label

15N-NMR characterization of His residues in and around the active site of FeSOD.

@en

15N-NMR characterization of His residues in and around the active site of FeSOD.

@nl

prefLabel

15N-NMR characterization of His residues in and around the active site of FeSOD.

@en

15N-NMR characterization of His residues in and around the active site of FeSOD.

@nl

P1476

15N-NMR characterization of His residues in and around the active site of FeSOD.

@en

P2093

Anne-Frances Miller

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

Emine Yikilmaz

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

Surekha Vathyam

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

P2860

Interrupting the hydrogen bond network at the active site of human manganese superoxide dismutase

Multiple replacements of glutamine 143 in human manganese superoxide dismutase: effects on structure, stability, and catalysis

Removing a hydrogen bond in the dimer interface of Escherichia coli manganese superoxide dismutase alters structure and reactivity

Catalytic and structural effects of amino acid substitution at histidine 30 in human manganese superoxide dismutase: insertion of valine C gamma into the substrate access channel

The structure of human mitochondrial manganese superoxide dismutase reveals a novel tetrameric interface of two 4-helix bundles

How can a single second sphere amino acid substitution cause reduction midpoint potential changes of hundreds of millivolts?

Structure-function in Escherichia coli iron superoxide dismutase: comparisons with the manganese enzyme from Thermus thermophilus

Probing the active site of human manganese superoxide dismutase: the role of glutamine 143

Raster3D: photorealistic molecular graphics

The 2-His-1-carboxylate facial triad: a versatile platform for dioxygen activation by mononuclear non-heme iron(II) enzymes.

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275-284

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scholarly article

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10.1016/J.BBAPAP.2009.11.009

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P932

6011655

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15N-NMR characterization of His residues in and around the active site of FeSOD.

about

P2860

P2860

15N-NMR characterization of His residues in and around the active site of FeSOD.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P577

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P577

P698

P932