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The History of Animal and Plant Sulfite Oxidase—A Personal View

Sulfite oxidase is one of five molybdenum-containing enzymes known in eukaryotes where it catalyzes the oxidation of sulfite to sulfate. This review covers the history of sulfite oxidase research starting out with the early years of its discovery as a hepatic mitochondrial enzyme in vertebrates, lea...

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Autores principales: Mendel, Ralf R., Schwarz, Günter
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10574614/
https://www.ncbi.nlm.nih.gov/pubmed/37836841
http://dx.doi.org/10.3390/molecules28196998
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author Mendel, Ralf R.
Schwarz, Günter
author_facet Mendel, Ralf R.
Schwarz, Günter
author_sort Mendel, Ralf R.
collection PubMed
description Sulfite oxidase is one of five molybdenum-containing enzymes known in eukaryotes where it catalyzes the oxidation of sulfite to sulfate. This review covers the history of sulfite oxidase research starting out with the early years of its discovery as a hepatic mitochondrial enzyme in vertebrates, leading to basic biochemical and structural properties that have inspired research for decades. A personal view on sulfite oxidase in plants, that sulfates are assimilated for their de novo synthesis of cysteine, is presented by Ralf Mendel with numerous unexpected findings and unique properties of this single-cofactor sulfite oxidase localized to peroxisomes. Guenter Schwarz connects his research to sulfite oxidase via its deficiency in humans, demonstrating its unique role amongst all molybdenum enzymes in humans. In essence, in both the plant and animal kingdoms, sulfite oxidase represents an important player in redox regulation, signaling and metabolism, thereby connecting sulfur and nitrogen metabolism in multiple ways.
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spelling pubmed-105746142023-10-14 The History of Animal and Plant Sulfite Oxidase—A Personal View Mendel, Ralf R. Schwarz, Günter Molecules Review Sulfite oxidase is one of five molybdenum-containing enzymes known in eukaryotes where it catalyzes the oxidation of sulfite to sulfate. This review covers the history of sulfite oxidase research starting out with the early years of its discovery as a hepatic mitochondrial enzyme in vertebrates, leading to basic biochemical and structural properties that have inspired research for decades. A personal view on sulfite oxidase in plants, that sulfates are assimilated for their de novo synthesis of cysteine, is presented by Ralf Mendel with numerous unexpected findings and unique properties of this single-cofactor sulfite oxidase localized to peroxisomes. Guenter Schwarz connects his research to sulfite oxidase via its deficiency in humans, demonstrating its unique role amongst all molybdenum enzymes in humans. In essence, in both the plant and animal kingdoms, sulfite oxidase represents an important player in redox regulation, signaling and metabolism, thereby connecting sulfur and nitrogen metabolism in multiple ways. MDPI 2023-10-09 /pmc/articles/PMC10574614/ /pubmed/37836841 http://dx.doi.org/10.3390/molecules28196998 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Mendel, Ralf R.
Schwarz, Günter
The History of Animal and Plant Sulfite Oxidase—A Personal View
title The History of Animal and Plant Sulfite Oxidase—A Personal View
title_full The History of Animal and Plant Sulfite Oxidase—A Personal View
title_fullStr The History of Animal and Plant Sulfite Oxidase—A Personal View
title_full_unstemmed The History of Animal and Plant Sulfite Oxidase—A Personal View
title_short The History of Animal and Plant Sulfite Oxidase—A Personal View
title_sort history of animal and plant sulfite oxidase—a personal view
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10574614/
https://www.ncbi.nlm.nih.gov/pubmed/37836841
http://dx.doi.org/10.3390/molecules28196998
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