Elucidating substrate binding in the light-dependent protochlorophyllide oxidoreductase-Reference-Cited by-同舟云学术

Elucidating substrate binding in the light-dependent protochlorophyllide oxidoreductase

Published:2024 Issue:20 Volume:15 Page:7767-7780
ISSN:2041-6520
Container-title:Chemical Science
language:en
Short-container-title:Chem. Sci.

Author:

Pesara Penelope¹,Szafran Katarzyna²,Nguyen Henry C.³,Sirohiwal Abhishek⁴,Pantazis Dimitrios A.¹^ORCID,Gabruk Michal²^ORCID

Affiliation:

1. Max-Planck-Institut für Kohlenforschung, Kaiser-Wilhelm-Platz 1, 45470, Mülheim an der Ruhr, Germany

2. Department of Plant Physiology and Biochemistry, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Gronostajowa 7, 30-387, Cracow, Poland

3. Department of Biochemistry & Biophysics, Quantitative Biosciences Institute, University of California, San Francisco, CA, USA

4. Department of Biochemistry and Biophysics, Arrhenius Laboratory, Stockholm University, 10691, Stockholm, Sweden

Abstract

Two protochlorophyllide binding modes to the light-dependent protochlorophyllide oxidoreductase were considered: mode B exhibits more thermodynamically favorable binding.

Funder

Narodowe Centrum Nauki

Uniwersytet Jagielloński w Krakowie

Publisher

Royal Society of Chemistry (RSC)

Link

http://pubs.rsc.org/en/content/articlepdf/2024/SC/D4SC00923A

Reference38 articles.

1. Post-translational regulation of metabolic checkpoints in plant tetrapyrrole biosynthesis

2. Light-Dependent Protochlorophyllide Oxidoreductase: Phylogeny, Regulation, and Catalytic Properties

3. Regulation and function of tetrapyrrole biosynthesis in plants and algae

4. Regulation and evolution of chlorophyll metabolism

5. Ultrafast catalytic processes and conformational changes in the light-driven enzyme protochlorophyllide oxidoreductase (POR)

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