Role of calcium in metalloenzymes: effects of calcium removal on the axial ligation geometry and magnetic properties of the catalytic diheme center in MauG. (Q35804440)

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scientific article published on 16 February 2012

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English	Role of calcium in metalloenzymes: effects of calcium removal on the axial ligation geometry and magnetic properties of the catalytic diheme center in MauG.	scientific article published on 16 February 2012

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scholarly article

1 reference

Europe PubMed Central

PMC publication ID

10 August 2017

Role of calcium in metalloenzymes: effects of calcium removal on the axial ligation geometry and magnetic properties of the catalytic diheme center in MauG. (English)

1 reference

Europe PubMed Central

PMC publication ID

10 August 2017

object named as

Shenghui Xue

6

0 references

object named as

Aimin Liu

9

0 references

Victor L. Davidson

object named as

Victor L Davidson

8

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author name string

Yan Chen

1

1 reference

Europe PubMed Central

PMC publication ID

10 August 2017

Sunil G Naik

2

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Europe PubMed Central

PMC publication ID

10 August 2017

J Krzystek

3

1 reference

Europe PubMed Central

PMC publication ID

10 August 2017

Sooim Shin

4

1 reference

Europe PubMed Central

PMC publication ID

10 August 2017

William H Nelson

5

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Europe PubMed Central

PMC publication ID

10 August 2017

Jenny J Yang

7

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Europe PubMed Central

PMC publication ID

10 August 2017

language of work or name

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publication date

16 February 2012

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Europe PubMed Central

PMC publication ID

10 August 2017

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Europe PubMed Central

PMC publication ID

10 August 2017

51

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Europe PubMed Central

PMC publication ID

10 August 2017

8

1 reference

Europe PubMed Central

PMC publication ID

10 August 2017

1586-1597

1 reference

Europe PubMed Central

PMC publication ID

10 August 2017

Crystal Structures of CO and NO Adducts of MauG in Complex with Pre-Methylamine Dehydrogenase: Implications for the Mechanism of Dioxygen Activation

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3294375

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Functional Importance of Tyrosine 294 and the Catalytic Selectivity for the Bis-Fe(IV) State of MauG Revealed by Replacement of This Axial Heme Ligand with Histidine,

1 reference

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In Crystallo Posttranslational Modification Within a MauG/Pre-Methylamine Dehydrogenase Complex

1 reference

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Review: studies of ferric heme proteins with highly anisotropic/highly axial low spin (S = 1/2) electron paramagnetic resonance signals with bis-histidine and histidine-methionine axial iron coordination

1 reference

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A catalytic di-heme bis-Fe(IV) intermediate, alternative to an Fe(IV)=O porphyrin radical

1 reference

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Redox-linked structural changes associated with the formation of a catalytically competent form of the diheme cytochrome c peroxidase from Pseudomonas aeruginosa

1 reference

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1 reference

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Models of the membrane-bound cytochromes: mössbauer spectra of crystalline low-spin ferriheme complexes having axial ligand plane dihedral angles ranging from 0 degree to 90 degrees

1 reference

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Structural basis for the mechanism of Ca(2+) activation of the di-heme cytochrome c peroxidase from Pseudomonas nautica 617.

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Further insights into quinone cofactor biogenesis: probing the role of mauG in methylamine dehydrogenase tryptophan tryptophylquinone formation

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Models of the bis-histidine-ligated electron-transferring cytochromes. Comparative geometric and electronic structure of low-spin ferro- and ferrihemes

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The tightly bound calcium of MauG is required for tryptophan tryptophylquinone cofactor biosynthesis

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Identifiers

10.1021/BI201575F

1 reference

Europe PubMed Central

PMC publication ID

10 August 2017

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

10 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

10 August 2017

ResearchGate publication ID

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