(Q50025110)

23 February 2018

title

Protein motions are coupled to the reaction chemistry in coenzyme B12-dependent ethanolamine ammonia lyase. (English)

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23 February 2018

author

Alex R. Jones

2

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23 February 2018

Sam Hay

3

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23 February 2018

Mike Towrie

5

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23 February 2018

Nigel Scrutton

6

object named as

Nigel S Scrutton

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23 February 2018

author name string

Henry J Russell

1

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23 February 2018

Gregory M Greetham

4

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23 February 2018

language of work or name

English

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publication date

15 August 2012

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23 February 2018

Angewandte Chemie International Edition

published in

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volume

51

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23 February 2018

issue

37

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23 February 2018

page(s)

9306-9310

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Chemistry and enzymology of vitamin B12.

cites work

1 reference

https://api.crossref.org/works/10.1002%2FANIE.201202502

Adenosyl radical: reagent and catalyst in enzyme reactions.

21 January 2018

1 reference

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Magnetic field effect studies indicate reduced geminate recombination of the radical pair in substrate-bound adenosylcobalamin-dependent ethanolamine ammonia lyase

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FANIE.201202502

Good vibrations in enzyme-catalysed reactions

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FANIE.201202502

Taking Ockham's razor to enzyme dynamics and catalysis

21 January 2018

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https://api.crossref.org/works/10.1002%2FANIE.201202502

Radical catalysis in coenzyme B12-dependent isomerization (eliminating) reactions

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FANIE.201202502

Isotope effects in the transient phases of the reaction catalyzed by ethanolamine ammonia-lyase: determination of the number of exchangeable hydrogens in the enzyme-cofactor complex.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FANIE.201202502

Continuous wave photolysis magnetic field effect investigations with free and protein-bound alkylcobalamins

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FANIE.201202502

Identification of the substrate radical intermediate derived from ethanolamine during catalysis by ethanolamine ammonia-lyase

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FANIE.201202502

Conformational changes on substrate binding to methylmalonyl CoA mutase and new insights into the free radical mechanism

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FANIE.201202502

Substrate-induced conformational change of a coenzyme B12-dependent enzyme: crystal structure of the substrate-free form of diol dehydratase

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FANIE.201202502

Large-scale Domain Dynamics and Adenosylcobalamin Reorientation Orchestrate Radical Catalysis in Ornithine 4,5-Aminomutase

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FANIE.201202502

Crystal Structures of Ethanolamine Ammonia-lyase Complexed with Coenzyme B12 Analogs and Substrates

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FANIE.201202502

Characterization of protein contributions to cobalt-carbon bond cleavage catalysis in adenosylcobalamin-dependent ethanolamine ammonia-lyase by using photolysis in the ternary complex

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2FANIE.201202502

Ultrafast infrared spectral fingerprints of vitamin B12 and related cobalamins

21 January 2018

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Stopped-flow Fourier transform infrared spectroscopy allows continuous monitoring of azide reduction, carbon monoxide inhibition, and ATP hydrolysis by nitrogenase

21 January 2018

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https://api.crossref.org/works/10.1002%2FANIE.201202502

Role of aspartate-96 in proton translocation by bacteriorhodopsin.

21 January 2018

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Femtosecond infrared spectroscopy of bacteriorhodopsin chromophore isomerization

21 January 2018

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Photolysis and recombination of adenosylcobalamin bound to glutamate mutase.

21 January 2018

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21 January 2018

Identifiers

DOI

10.1002/ANIE.201202502

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23 February 2018

PubMed ID

22893270

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23 February 2018