Protonation States of the Tryptophan Synthase Internal Aldimine Active Site from Solid-State NMR Spectroscopy: Direct Observation of the Protonated Schiff Base Linkage to Pyridoxal-5′-Phosphate-Reference-Cited by-同舟云学术

Protonation States of the Tryptophan Synthase Internal Aldimine Active Site from Solid-State NMR Spectroscopy: Direct Observation of the Protonated Schiff Base Linkage to Pyridoxal-5′-Phosphate

Published:2014-09-03 Issue:37 Volume:136 Page:12824-12827
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Caulkins Bethany G.¹,Bastin Baback¹,Yang Chen¹,Neubauer Thomas J.¹,Young Robert P.¹,Hilario Eduardo²,Huang Yu-ming M.¹,Chang Chia-en A.¹,Fan Li²,Dunn Michael F.²,Marsella Michael J.¹,Mueller Leonard J.¹

Affiliation:

1. Department of Chemistry, University of California, Riverside, California 92521, United States

2. Department of Biochemistry, University of California, Riverside, California 92521, United States

Funder

U.S. Department of Education

National Institute of General Medical Sciences

Division of Graduate Education

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja506267d

Reference46 articles.

1. A General Mechanism for Vitamin B6-catalyzed Reactions1

2. Controlling reaction specificity in pyridoxal phosphate enzymes

3. An Improved Broadband Decoupling Sequence for Liquid Crystals and Solids

4. Semicarbazone Formation from Pyridoxal, Pyridoxal Phosphate, and Their Schiff Bases

5. Pyridoxine and Pyridoxal Analogs. VII. Acid-Base Equilibria of Schiff Bases

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