Plant Protochlorophyllide Oxidoreductases A and B

Garrone, Alessio; Archipowa, Nataliya; Zipfel, Peter F.; Hermann, Gudrun; Dietzek, Benjamin

doi:10.1074/jbc.m115.663161

Cited by 36 publications

(17 citation statements)

References 47 publications

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“…PORs originating from a variety of photosynthetic organisms, including cyanobacteria and higher plants, have been studied in detail using ultrafast and cryogenic spectroscopic techniques [8] , [16] , [18] , [19] , [20] , [21] . Excited state interactions between the Pchlide molecule and active site residues in the enzyme are proposed to result in a reactive charge-separated state that facilitates the sequential hydride and proton transfer reactions on a microsecond timescale [7] , [15] , [18] , [22] .…”

Section: Introductionmentioning

confidence: 99%

Multiple active site residues are important for photochemical efficiency in the light-activated enzyme protochlorophyllide oxidoreductase (POR)

Menon

Hardman

Scrutton

et al. 2016

Journal of Photochemistry and Photobiology B: Biology

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Protochlorophyllide oxidoreductase (POR) catalyzes the light-driven reduction of protochlorophyllide (Pchlide), an essential, regulatory step in chlorophyll biosynthesis. The unique requirement of the enzyme for light has provided the opportunity to investigate how light energy can be harnessed to power biological catalysis and enzyme dynamics. Excited state interactions between the Pchlide molecule and the protein are known to drive the subsequent reaction chemistry. However, the structural features of POR and active site residues that are important for photochemistry and catalysis are currently unknown, because there is no crystal structure for POR. Here, we have used static and time-resolved spectroscopic measurements of a number of active site variants to study the role of a number of residues, which are located in the proposed NADPH/Pchlide binding site based on previous homology models, in the reaction mechanism of POR. Our findings, which are interpreted in the context of a new improved structural model, have identified several residues that are predicted to interact with the coenzyme or substrate. Several of the POR variants have a profound effect on the photochemistry, suggesting that multiple residues are important in stabilizing the excited state required for catalysis. Our work offers insight into how the POR active site geometry is finely tuned by multiple active site residues to support enzyme-mediated photochemistry and reduction of Pchlide, both of which are crucial to the existence of life on Earth.

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Section: Introductionmentioning

confidence: 99%

Multiple active site residues are important for photochemical efficiency in the light-activated enzyme protochlorophyllide oxidoreductase (POR)

Menon

Hardman

Scrutton

et al. 2016

Journal of Photochemistry and Photobiology B: Biology

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“…[7] Although light-dependent enzymes that directly utilize visible light as an energy source are highly sought after, photoenzymes have seldom been found in nature.The activities of these type of enzymes depend on the irradiation of the cofactor in the active site with light, such as in DNA-repair enzymes [8] and protochlorophyllide oxidoreductases. [9] Very recently,Beisson and co-workers discovered af atty acid photodecarboxylase from Chlorella variabilis NC64A (CvFAP), which they used to convert long-chain fatty acids into hydrocarbons. [9] In another key study,H ollmanns group reported the synthesis of alkanes from triglycerides through ad esigned lipase/CvFAP-catalyzed cascade reaction.…”

mentioning

confidence: 99%

“…[9] Very recently,Beisson and co-workers discovered af atty acid photodecarboxylase from Chlorella variabilis NC64A (CvFAP), which they used to convert long-chain fatty acids into hydrocarbons. [9] In another key study,H ollmanns group reported the synthesis of alkanes from triglycerides through ad esigned lipase/CvFAP-catalyzed cascade reaction. [11a] Thed ifferent activity of cis-a nd trans-oleic acid mentioned in these reports strongly aroused our interest.…”

mentioning

confidence: 99%

Light‐Driven Kinetic Resolution of α‐Functionalized Carboxylic Acids Enabled by an Engineered Fatty Acid Photodecarboxylase

Fan

et al. 2019

Angew Chem Int Ed

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Chiral a-functionalized carboxylic acids are valuable precursors for avariety of medicines and natural products. Herein, we described an engineered fatty acid photodecarboxylase (CvFAP)-catalyzed kinetic resolution of a-amino acids and a-hydroxy acids,w hich provides the unreacted R-configured substrates with high yields and excellent stereoselectivity (ee up to 99 %). This efficient light-driven process requires neither NADPH recycling nor prior preparation of esters, which were required in previous biocatalytic approaches.T he structure-guided engineering strategy is based on the scanning of large amino acids at hotspots to narrowthe substrate binding tunnel. To the best of our knowledge,this is the first example of asymmetric catalysis by an engineered CvFAP.

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“…The up-regulation of genes encoding for enzymes active in the detoxification mechanism of aldehydes (aldehyde dehydrogenases and aldo/ketoreductases) is consistent with the altered redox state of zucchini infested plants ( Kishimoto et al, 2005 ; Laluk et al, 2011 ; Kim and Hwang, 2015 ; Sengupta et al, 2015 ). POR is an essential enzyme that catalyzes the photoreduction of protochlorophyllide to chlorophyllide, which is ultimately converted into chlorophyll in developing leaves ( Garrone et al, 2015 ). However, this enzyme is also involved in oxidative stress, reducing plasma membrane damage in Arabidopsis and its over-expression was also associated with resistance to biotic stress ( Tripathy, 2009 ; Pattanayak and Tripathy, 2011 ).…”

Section: Discussionmentioning

confidence: 99%

Zucchini Plants Alter Gene Expression and Emission of (E)-β-Caryophyllene Following Aphis gossypii Infestation

et al. 2021

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Zucchini (Cucurbita pepo L.) is widely cultivated in temperate regions. One of the major production challenges is the damage caused by Aphis gossypii (Homoptera: Aphididae), a polyphagous aphid, which can negatively affect its host plant, both directly by feeding and indirectly by vectoring viruses. To gain insights into the transcriptome events that occur during the zucchini–aphid interaction and to understand the early-to-late defense response through gene expression profiles, we performed RNA-sequencing (RNA-Seq) on zucchini leaves challenged by A. gossypii (24, 48, and 96 h post-infestation; hpi). Data analysis indicated a complex and dynamic pattern of gene expression and a transient transcriptional reconfiguration that involved more than 700 differentially expressed genes (DEGs), including a large number of defense-related genes. The down-regulation of key genes of plant immunity, such as leucine-rich repeat (LRR) protein kinases, transcription factors, and genes associated with direct (i.e., protease inhibitors, cysteine peptidases, etc.) and indirect (i.e., terpene synthase) defense responses, suggests the aphid ability to manipulate plant immune responses. We also investigated the emission of volatile organic compounds (VOCs) from infested plants and observed a reduced emission of (E)-β-caryophyllene at 48 hpi, likely the result of aphid effectors, which reflects the down-regulation of two genes involved in the biosynthesis of terpenoids. We showed that (E)-β-caryophyllene emission was modified by the duration of plant infestation and by aphid density and that this molecule highly attracts Aphidius colemani, a parasitic wasp of A. gossypii. With our results we contributed to the identification of genes involved in cucurbit plant interactions with phloem feeders. Our findings may also help pave the way toward developing tolerant zucchini varieties and to identify molecules for sustainable management of harmful insect populations.

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Plant Protochlorophyllide Oxidoreductases A and B

Cited by 36 publications

References 47 publications

Multiple active site residues are important for photochemical efficiency in the light-activated enzyme protochlorophyllide oxidoreductase (POR)

Multiple active site residues are important for photochemical efficiency in the light-activated enzyme protochlorophyllide oxidoreductase (POR)

Light‐Driven Kinetic Resolution of α‐Functionalized Carboxylic Acids Enabled by an Engineered Fatty Acid Photodecarboxylase

Zucchini Plants Alter Gene Expression and Emission of (E)-β-Caryophyllene Following Aphis gossypii Infestation

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