Electron Paramagnetic Resonance Spectroscopic Identification of the Fe–S Clusters in the SPASM Domain-Containing Radical SAM Enzyme PqqE-Reference-Cited by-同舟云学术

Electron Paramagnetic Resonance Spectroscopic Identification of the Fe–S Clusters in the SPASM Domain-Containing Radical SAM Enzyme PqqE

Published:2019-11-26 Issue:51 Volume:58 Page:5173-5187
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Tao Lizhi¹^ORCID,Zhu Wen²^ORCID,Klinman Judith P.²^ORCID,Britt R. David¹^ORCID

Affiliation:

1. Department of Chemistry, University of California, Davis, California 95616, United States

2. Department of Chemistry, Department of Molecular and Cell Biology, and California Institute for Quantitative Biosciences, University of California, Berkeley, California 94720, United States

Funder

National Institutes of Health

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.9b00960

Reference59 articles.

1. The PQQ story

2. Pyrroloquinoline Quinone (PQQ) and Quinoprotein Enzymes

3. Intrigues and Intricacies of the Biosynthetic Pathways for the Enzymatic Quinocofactors: PQQ, TTQ, CTQ, TPQ, and LTQ

4. Increased production of recombinant pyrroloquinoline quinone (PQQ) glucose dehydrogenase by metabolically engineered Escherichia coli strain capable of PQQ biosynthesis

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3. Radical SAM Enzyme PylB Generates a Lysyl Radical Intermediate in the Biosynthesis of Pyrrolysine by Using SAM as a Cofactor;Journal of the American Chemical Society;2024-03-01

4. Hydrogen–Deuterium Exchange Mass Spectrometry Identifies Local and Long-Distance Interactions within the Multicomponent Radical SAM Enzyme, PqqE;ACS Central Science;2024-01-17

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