Mechanistic Interpretation of Tryptophan Fluorescence Quenching in the Time Courses of Glutamate Dehydrogenase Catalyzed Reactions-Reference-Cited by-同舟云学术

Mechanistic Interpretation of Tryptophan Fluorescence Quenching in the Time Courses of Glutamate Dehydrogenase Catalyzed Reactions

Published:1996-01-01 Issue:51 Volume:35 Page:16483-16488
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Saha Swapan K.¹,Maniscalco Steven J.¹,Fisher Harvey F.¹

Affiliation:

1. Laboratory of Molecular Biochemistry, Veterans Affairs Medical Center, and Department of Biochemistry, University of Kansas Medical Center, Kansas City, Missouri 64128

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi9612531

Reference19 articles.

1. The mechanism of substrate and coenzyme binding to clostridial glutamate dehydrogenase during oxidative deamination

2. Pulse fluorimetry study of energy transfers between tryptophan residues and NADPH in beef liver glutamate dehydrogenase complexes

3. Kinetics of ligand binding to dihydrofolate reductase: binary complex formation with NADPH and coenzyme analogues

4. Interpretation of Transient-State Kinetic Isotope Effects

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