Plant molybdoenzymes and their response to stress

Zdunek‐Zastocka, Edyta; Lips, Herman

doi:10.1007/s11738-003-0026-z

Cited by 12 publications

(7 citation statements)

References 129 publications

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“…In A. thaliana there are four genes, AOX1-4 [154,155], with AOX3 specifically involved in abscissic acid biosynthesis in leaves (but not seeds) [154,156]. In Pisum sativum , there are three genes encoding aldehyde oxidases, Psaox1-3 , the last appearing to encode a stress-specific abscissic aldehyde oxidase [157]. None of the plant enzymes have been studied in great detail at a biochemical level, but by analogy to other enzymes of this family considerable overlap in substrate specificity among the plant aldehyde oxidases is to be expected.…”

Section: Aldehyde Oxidasementioning

confidence: 99%

Molybdenum enzymes in higher organisms

Hille

Nishino

Bittner

2011

Coordination Chemistry Reviews

206

184

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Section: Aldehyde Oxidasementioning

confidence: 99%

Molybdenum enzymes in higher organisms

Hille

Nishino

Bittner

2011

Coordination Chemistry Reviews

206

184

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“…The crucial component of molybdoenzymes is a structure called the molybdenum cofactor (Moco) [14] that forms the active site of the molybdoenzyme. In Moco, a pterin, known as molybdopterin (MPT), serves as a scaffold for the molybdenum atom.…”

Section: Introductionmentioning

confidence: 99%

Optimization of overexpression of a chaperone protein of steroid C25 dehydrogenase for biochemical and biophysical characterization

Niedzialkowska

Mrugala

Rugor

et al. 2017

Protein Expression and Purification

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Molybdenum is an essential nutrient for metabolism in plant, bacteria, and animals. Molybdoenzymes are involved in nitrogen assimilation and oxidoreductive detoxification, and bioconversion reactions of environmental, industrial, and pharmaceutical interest. Molybdoenzymes contain a molybdenum cofactor (Moco), which is a pyranopterin heterocyclic compound that binds a molybdenum atom via a dithiolene group. Because Moco is a large and complex compound deeply buried within the protein, molybdoenzymes are accompanied by private chaperone proteins responsible for the cofactor’s insertion into the enzyme and the enzyme’s maturation. An efficient recombinant expression and purification of both Moco-free and Moco-containing molybdoenzymes and their chaperones is of paramount importance for fundamental and applied research related to molybdoenzymes. In this work, we focused on a D1 protein annotated as a chaperone of steroid C25 dehydrogenase (S25DH) from Sterolibacterium denitrificans Chol-1S. The D1 protein is presumably involved in the maturation of S25DH engaged in oxygen-independent oxidation of sterols. As this chaperone is thought to be a crucial element that ensures the insertion of Moco into the enzyme and consequently, proper folding of S25DH optimization of the chaperon’s expression is the first step toward the development of recombinant expression and purification methods for S25DH. We have identified common E. coli strains and conditions for both expression and purification that allow us to selectively produce Moco-containing and Moco-free chaperones. We have also characterized the Moco-containing chaperone by EXAFS and HPLC analysis and identified conditions that stabilize both forms of the protein. The protocols presented here are efficient and result in protein quantities sufficient for biochemical studies.

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“…Molybdoenzymes in plants are the key molybdoenzymess in nitrate assimilation, purine metabolism, hormone biosynthesis, and most likely, sulfite detoxication. It is believed that they take part in the process of stress adaptation and, as a result understanding of the way they react in environmental stressful situations is vital for agriculture and for plant stress resistance improvement [9].…”

Section: Introductionmentioning

confidence: 99%

Molybdoenzyme Participation In Plant Biochemical Processes

Tokasheva¹,

Nurbekova²,

Akbassova³

et al. 2021

Eurasian Journal of Applied Biotechnology

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Molybdenum is a key microelement in plant vital functioning. The microelement can be absorbed by the plants only in the form of molybdate-anion. The Molybdenum deficiency affects negatively to the most important agricultural growing. As molybdenum takes part in such vital mechanisms as nitrogen and sulfur metabolism, plant hormone biosynthesis, and purine banding catabolism. Molybdenum is included in enzyme content which is called molybdoenzyms. Having bonded with molybdopterin it creates molybdenum co-factor (Moco) and gets oxidation-reduction properties. Moco is included in active site of molybdoenzymes. They take part in sulfur and nitrogen metabolism, and detrimental compound detoxication. Molybdenum deficiency is characterized by the slow plant growth, low amount of chlorophyll ascorbic acid capacity.It was noticed that plants suffering from the molybdenum deficiency can be saved, sodium molibdate can be used, it can be put directly in the soil or plant leaves can sprayed with the solution. There are five plant molibdoenzymes which are currently known: sulfite oxidase (SO), xanthine dehydrogenase (XD), nitrate reductase (NR), aldehyde oxidase (AO) and mitochondrial amidoxim-regenerative component. Nitrate reductase catalyzes the first stage of nitrate assimilation, eucariotic organisms contain three isoforms of the molybdoezimes: A NADH, A NAD(P)H и NADPH. Xanthine dehydrogenase regulates purine metabolism. XD increases plant antioxidant ability and slows down leaves aging. Molybdoenzymess are involved in the process of the stress adaptation, defining of the mechanisms and their reaction to environmental stress conditions is important for plant stress resistance.

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Plant molybdoenzymes and their response to stress

Cited by 12 publications

References 129 publications

Molybdenum enzymes in higher organisms

Molybdenum enzymes in higher organisms

Optimization of overexpression of a chaperone protein of steroid C25 dehydrogenase for biochemical and biophysical characterization

Molybdoenzyme Participation In Plant Biochemical Processes

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