(Q27660923)

1

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Natasha Yeung

2

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Yi-Gui Gao

3

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Kyle D Miner

4

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Shiliang Tian

5

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Howard Robinson

Proceedings of the National Academy of Sciences of the United States of America

6

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language of work or name

English

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publication date

11 May 2010

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published in

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volume

107

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issue

19

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page(s)

8581-6

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cites work

Rational design of a structural and functional nitric oxide reductase

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Rationally tuning the reduction potential of a single cupredoxin beyond the natural range

20 March 2017

1 reference

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Design and engineering of an O(2) transport protein

20 March 2017

1 reference

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De novo computational design of retro-aldol enzymes

20 March 2017

1 reference

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Characterization of a helical protein designed from first principles

20 March 2017

1 reference

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Designing artificial enzymes by intuition and computation

20 March 2017

1 reference

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Design strategies for the creation of artificial metalloenzymes.

29 September 2017

1 reference

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Design of functional metalloproteins

29 September 2017

1 reference

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The bacterial respiratory nitric oxide reductase

29 September 2017

1 reference

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Accommodation of two diatomic molecules in cytochrome bo: insights into NO reductase activity in terminal oxidases

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2889330

Vectorial proton transfer coupled to reduction of O2 and NO by a heme-copper oxidase

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2889330

A functional nitric oxide reductase model

29 September 2017

1 reference

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One heme, diverse functions: using biosynthetic myoglobin models to gain insights into heme-copper oxidases and nitric oxide reductases

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2889330

Looking for the minimum common denominator in haem-copper oxygen reductases: towards a unified catalytic mechanism

29 September 2017

1 reference

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Spectroscopic characterization of heme iron-nitrosyl species and their role in NO reductase mechanisms in diiron proteins.

29 September 2017

1 reference

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Computational protein design: structure, function and combinatorial diversity

29 September 2017

1 reference

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A new assay for nitric oxide reductase reveals two conserved glutamate residues form the entrance to a proton-conducting channel in the bacterial enzyme.

29 September 2017

1 reference

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Catalytic reduction of NO to N2O by a designed heme copper center in myoglobin: implications for the role of metal ions

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2889330

Nitric oxide signaling: no longer simply on or off.

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2889330

Probing metal-protein interactions using a de novo design approach

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2889330

NO reduction by nitric-oxide reductase from denitrifying bacterium Pseudomonas aeruginosa: characterization of reaction intermediates that appear in the single turnover cycle

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2889330

De novo design of catalytic proteins

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2889330

29 September 2017

Heme protein assemblies

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2889330

Biological inorganic chemistry at the beginning of the 21st century

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2889330

The role of copper and protons in heme-copper oxidases: kinetic study of an engineered heme-copper center in myoglobin

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2889330

Nitric oxide in biological denitrification: Fe/Cu metalloenzyme and metal complex NO(x) redox chemistry

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2889330

Proton and electron pathways in the bacterial nitric oxide reductase

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2889330

Two conserved glutamates in the bacterial nitric oxide reductase are essential for activity but not assembly of the enzyme

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2889330

Heme-copper assembly mediated reductive coupling of nitrogen monoxide (*NO).

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2889330

Active-site models of bacterial nitric oxide reductase featuring tris-histidyl and glutamic acid mimics: influence of a carboxylate ligand on Fe(B) binding and the heme Fe/Fe(B) redox potential

2 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2889330

The active site of the bacterial nitric oxide reductase is a dinuclear iron center

2 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2889330

Engineering metal-binding sites in proteins

2 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2889330

Determination of heme a concentration in cytochrome preparations by hemochromogen method.

2 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2889330

De novo design, expression, and characterization of Felix: a four-helix bundle protein of native-like sequence

2 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2889330

Genomic DNA cloning of the region encoding nitric oxide reductase in Paracoccus halodenitrificans and a structure model relevant to cytochrome oxidase.

2 June 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.1000526107

Exploring the terminal region of the proton pathway in the bacterial nitric oxide reductase

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.1000526107

The cytochrome cbb3 from Pseudomonas stutzeri displays nitric oxide reductase activity

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.1000526107

Defining the proton entry point in the bacterial respiratory nitric-oxide reductase

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.1000526107

Synthesis and spectroscopy of micro-oxo (O(2)(-))-bridged heme/non-heme diiron complexes: models for the active site of nitric oxide reductase

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.1000526107

Heme/non-heme diiron(II) complexes and O2, CO, and NO adducts as reduced and substrate-bound models for the active site of bacterial nitric oxide reductase.

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.1000526107

Intermediates involved in the two electron reduction of NO to N2O by a functional synthetic model of heme containing bacterial NO reductase

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.1000526107

A functional model of the cytochrome c oxidase active site: unique conversion of a heme-mu-peroxo-Cu(II) intermediate into heme- superoxo/Cu(I).

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.1000526107

Heme-copper/dioxygen adduct formation relevant to cytochrome c oxidase: spectroscopic characterization of [(6L)FeIII-(O2(2-))-CuII]+.

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.1000526107

EPR and ENDOR studies of Fe(II) hemoproteins reduced and oxidized at 77 K.

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.1000526107

Effects of metal ions in the CuB center on the redox properties of heme in heme-copper oxidases: spectroelectrochemical studies of an engineered heme-copper center in myoglobin

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.1000526107

Trans effects in nitric oxide binding to myoglobin cavity mutant H93G.

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.1000526107

Photolysis of the HNO adduct of myoglobin: transient generation of the aminoxyl radical

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.1000526107

Iron-porphyrin NO complexes with covalently attached N-donor ligands: formation of a stable six-coordinate species in solution

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.1000526107

Design and synthesis of multi-haem proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.1000526107

Roles of four iron centers in Paracoccus halodenitrificans nitric oxide reductase

21 January 2018

1 reference

12 December 2020

Anaerobic oxidations of myoglobin and hemoglobin by spectroelectrochemistry

1 reference

12 December 2020

Resonance Raman detection of a ferrous five-coordinate nitrosylheme b(3) complex in cytochrome cbb(3) oxidase from Pseudomonas stutzeri

1 reference

12 December 2020

A low-redox potential heme in the dinuclear center of bacterial nitric oxide reductase: implications for the evolution of energy-conserving heme-copper oxidases

1 reference

12 December 2020

Reduction of nitric oxide in bacterial nitric oxide reductase--a theoretical model study

1 reference

12 December 2020

A pathway for protons in nitric oxide reductase from Paracoccus denitrificans

1 reference

12 December 2020

Resonance Raman spectroscopy of nitric oxide reductase and cbb(3) heme-copper oxidase

1 reference

12 December 2020

Ultrafast ligand binding dynamics in the active site of native bacterial nitric oxide reductase

1 reference

12 December 2020

Effects of buried ionizable amino acids on the reduction potential of recombinant myoglobin

1 reference

12 December 2020

Purification and initial kinetic and spectroscopic characterization of NO reductase from Paracoccus denitrificans

1 reference

12 December 2020

Isolation and characterization of nitric oxide reductase from Paracoccus halodenitrificans

1 reference

12 December 2020

release_lqbvgfvxxjcoxdbzfk7whxuhle

Identifiers

DOI

10.1073/PNAS.1000526107

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ADS bibcode

2010PNAS..107.8581L

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Fatcat ID

1 reference

Fatcat

https://api.fatcat.wiki/v0/release/lqbvgfvxxjcoxdbzfk7whxuhle

24 November 2022