ArticleThe Journal of biological chemistry2010
Mutagenesis alters the catalytic mechanism of the light-driven enzyme protochlorophyllide oxidoreductase.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 32 citations in OpenAlex.
- Structures of LPOR-Chlide complexes reveal the structural basis of membrane remodeling and photocatalysis.Nature communications · 2026Article
- The structural chemistry and biosynthesis of chlorophylls.RSC chemical biology · 2026Review
- Elucidating substrate binding in the light-dependent protochlorophyllide oxidoreductase.Chemical science · 2024Article
- An Alternative Proposal for the Reaction Mechanism of Light-Dependent Protochlorophyllide Oxidoreductase.ACS catalysis · 2022Article
- Complex Evolution of Light-Dependent Protochlorophyllide Oxidoreductases in Aerobic Anoxygenic Phototrophs: Origin, Phylogeny, and Function.Molecular biology and evolution · 2021Article
- Photocatalysis as the 'master switch' of photomorphogenesis in early plant development.Nature plants · 2021Review
- Crystal structures of cyanobacterial light-dependent protochlorophyllide oxidoreductase.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Stepwise Hydride Transfer in a Biological System: Insights into the Reaction Mechanism of the Light-Dependent Protochlorophyllide Oxidoreductase.Angewandte Chemie (International ed. in English) · 2018Article
- Multiple active site residues are important for photochemical efficiency in the light-activated enzyme protochlorophyllide oxidoreductase (POR).Journal of photochemistry and photobiology. B, Biology · 2016Article
- Differential Regulation of Duplicate Light-Dependent Protochlorophyllide Oxidoreductases in the Diatom Phaeodactylum tricornutum.PloS one · 2016Article
- Glutamate 338 is an electrostatic facilitator of C-Co bond breakage in a dynamic/electrostatic model of catalysis by ornithine aminomutase.The FEBS journal · 2015Article
- Extensive horizontal gene transfer, duplication, and loss of chlorophyll synthesis genes in the algae.BMC evolutionary biology · 2015Article
- Proteome-wide light/dark modulation of thiol oxidation in cyanobacteria revealed by quantitative site-specific redox proteomics.Molecular & cellular proteomics : MCP · 2014Article
- Engineering oxidoreductases: maquette proteins designed from scratch.Biochemical Society transactions · 2012Review
- A twin-track approach has optimized proton and hydride transfer by dynamically coupled tunneling during the evolution of protochlorophyllide oxidoreductase.The Journal of biological chemistry · 2011Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The light-activated enzyme protochlorophyllide oxidoreductase (POR) catalyzes an essential step in the synthesis of the most abundant pigment on Earth, chlorophyll. This unique reaction involves the sequential addition of a hydride and proton across the C17=C18 double bond of protochlorophyllide (Pchlide) by dynamically coupled quantum tunneling and is an important model system for studying the mechanism of hydrogen transfer reactions. In the present work, we have combined site-directed mutagenesis studies with a variety of sensitive spectroscopic and kinetic measurements to provide new insights into the mechanistic role of three universally conserved Cys residues in POR. We show that mutation of Cys-226 dramatically alters the catalytic mechanism of the enzyme. In contrast to wild-type POR, the characteristic charge-transfer intermediate, formed upon hydride transfer from NADPH to the C17 position of Pchlide, is absent in C226S variant enzymes. This suggests a concerted hydrogen transfer mechanism where proton transfer only is rate-limiting. Moreover, Pchlide reduction does not require the network of solvent-coupled conformational changes that play a key role in the proton transfer step of wild-type POR. We conclude that this globally important enzyme is finely tuned to facilitate efficient photochemistry, and the removal of a key interaction with Pchlide in the C226S variants significantly affects the local active site structure in POR, resulting in a shorter donor-acceptor distance for proton transfer.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.