Protein Motions Are Coupled to the Reaction Chemistry in Coenzyme B<sub>12</sub>‐Dependent Ethanolamine Ammonia Lyase

Russell, Henry J.; Jones, Alex R.; Hay, Sam; Greetham, Gregory M.; Towrie, Michael; Scrutton, Nigel S.

doi:10.1002/ange.201202502

Angewandte Chemie

2012

DOI: 10.1002/ange.201202502

|View full text |Cite

Protein Motions Are Coupled to the Reaction Chemistry in Coenzyme B₁₂‐Dependent Ethanolamine Ammonia Lyase

Henry J. Russell

Alex R. Jones

Sam Hay

et al.

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...

Citation Types

Supporting

Mentioning

Contrasting

Year Published

2013

2023

Publication Types

Select...

Article3

Relationship

Self Cite2

Independent1

Authors

Journals

Cited by 3 publications

(3 citation statements)

References 36 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…These motions occur both at the beginning and end of turnover, and accompany the homolysis and recombination processes illustrated in Scheme 1 . [ 9 ]…”

mentioning

confidence: 99%

“…Contact between E287 and 5′-deoxyadenosyl might be the origin of the ultrafast vibrational coupling observed between photoexcited B 12 and EAL. [ 9a ]…”

mentioning

confidence: 99%

“…There was also evidence for the involvement of more than one residue from our stopped-flow FTIR data that estimated the movement of approximately seven peptide bonds alongside the pre-steady-state chemistry. [ 9a ] Such a movement might not directly involve seven side chains, but does suggest a flexible, dynamic active site in EAL. This picture supports the model for Co–C bond homolysis in EAL proposed by Robertson et al: coordinated protein motions that guide the cleavage of the Co–C bond along the reaction coordinate.…”

mentioning

confidence: 99%

See 2 more Smart Citations

Dynamic, Electrostatic Model for the Generation and Control of High‐Energy Radical Intermediates by a Coenzyme B₁₂‐Dependent Enzyme

et al. 2013

Self Cite

View full text Add to dashboard Cite

show abstract

“…These motions occur both at the beginning and end of turnover, and accompany the homolysis and recombination processes illustrated in Scheme 1 . [ 9 ]…”

mentioning

confidence: 99%

“…Contact between E287 and 5′-deoxyadenosyl might be the origin of the ultrafast vibrational coupling observed between photoexcited B 12 and EAL. [ 9a ]…”

mentioning

confidence: 99%

mentioning

confidence: 99%

See 1 more Smart Citation

Dynamic, Electrostatic Model for the Generation and Control of High‐Energy Radical Intermediates by a Coenzyme B₁₂‐Dependent Enzyme

et al. 2013

Self Cite

View full text Add to dashboard Cite

show abstract

Probing Reversible Chemistry in Coenzyme B₁₂‐Dependent Ethanolamine Ammonia Lyase with Kinetic Isotope Effects

Jones

Rentergent

Scrutton

et al. 2015

Chemistry A European J

Self Cite

View full text Add to dashboard Cite

Coenzyme B12-dependent enzymes such as ethanolamine ammonia lyase have remarkable catalytic power and some unique properties that enable detailed analysis of the reaction chemistry and associated dynamics. By selectively deuterating the substrate (ethanolamine) and/or the β-carbon of the 5′-deoxyadenosyl moiety of the intrinsic coenzyme B12, it was possible to experimentally probe both the forward and reverse hydrogen atom transfers between the 5′-deoxyadenosyl radical and substrate during single-turnover stopped-flow measurements. These data are interpreted within the context of a kinetic model where the 5′-deoxyadenosyl radical intermediate may be quasi-stable and rearrangement of the substrate radical is essentially irreversible. Global fitting of these data allows estimation of the intrinsic rate constants associated with CoC homolysis and initial H-abstraction steps. In contrast to previous stopped-flow studies, the apparent kinetic isotope effects are found to be relatively small.

show abstract

Molecular Recognition Patterns between Vitamin B12 and Proteins Explored through STD-NMR and In Silico Studies

Ghosh

Thomas

Arcot

2023

Foods

View full text Add to dashboard Cite

Ligand–receptor molecular recognition is the basis of biological processes. The Saturation Transfer Difference–NMR (STD–NMR) technique has been recently used to gain qualitative and quantitative information about physiological interactions at an atomic resolution. The molecular recognition patterns between the cyanocobalamin (CNBL)/aqua cobalamin (OHBL) and different plant and animal proteins were investigated via STD–NMR supplemented by molecular docking. This study demonstrates that myoglobin has the highest binding affinity and that gluten has the lowest affinity. Casein also shows a higher binding affinity for cyanocobalamin when compared with that of plant-based proteins. STD–NMR results showed the moderate binding capability of casein with both CNBL and OHBL. Computer simulation confirmed the recognition mode in theory and was compared with the experiments. This work is beneficial for understanding the binding affinity and biological action of cyanocobalamin and will attract researchers to use NMR technology to link the chemical and physiological properties of nutrients.

show abstract

scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.

Contact Info

hi@scite.ai

10624 S. Eastern Ave., Ste. A-614

Henderson, NV 89052, USA

Blog Terms and Conditions API Terms Privacy Policy Contact Cookie Preferences Do Not Sell or Share My Personal Information

Made with 💙 for researchers

Part of the Research Solutions Family.

Protein Motions Are Coupled to the Reaction Chemistry in Coenzyme B₁₂‐Dependent Ethanolamine Ammonia Lyase

Cited by 3 publications

References 36 publications

Dynamic, Electrostatic Model for the Generation and Control of High‐Energy Radical Intermediates by a Coenzyme B₁₂‐Dependent Enzyme

Dynamic, Electrostatic Model for the Generation and Control of High‐Energy Radical Intermediates by a Coenzyme B₁₂‐Dependent Enzyme

Probing Reversible Chemistry in Coenzyme B₁₂‐Dependent Ethanolamine Ammonia Lyase with Kinetic Isotope Effects

Molecular Recognition Patterns between Vitamin B12 and Proteins Explored through STD-NMR and In Silico Studies

Contact Info

Product

Resources

About

Protein Motions Are Coupled to the Reaction Chemistry in Coenzyme B12‐Dependent Ethanolamine Ammonia Lyase

Cited by 3 publications

References 36 publications

Dynamic, Electrostatic Model for the Generation and Control of High‐Energy Radical Intermediates by a Coenzyme B12‐Dependent Enzyme

Dynamic, Electrostatic Model for the Generation and Control of High‐Energy Radical Intermediates by a Coenzyme B12‐Dependent Enzyme

Probing Reversible Chemistry in Coenzyme B12‐Dependent Ethanolamine Ammonia Lyase with Kinetic Isotope Effects

Molecular Recognition Patterns between Vitamin B12 and Proteins Explored through STD-NMR and In Silico Studies

Contact Info

Product

Resources

About

Protein Motions Are Coupled to the Reaction Chemistry in Coenzyme B₁₂‐Dependent Ethanolamine Ammonia Lyase

Dynamic, Electrostatic Model for the Generation and Control of High‐Energy Radical Intermediates by a Coenzyme B₁₂‐Dependent Enzyme

Dynamic, Electrostatic Model for the Generation and Control of High‐Energy Radical Intermediates by a Coenzyme B₁₂‐Dependent Enzyme

Probing Reversible Chemistry in Coenzyme B₁₂‐Dependent Ethanolamine Ammonia Lyase with Kinetic Isotope Effects