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亚硫酸盐氧化酶的历史——个人观点

The History of Animal and Plant Sulfite Oxidase-A Personal View.

机构信息

Institute of Plant Biology, Technical University Braunschweig, Humboldtstrasse 1, 38106 Braunschweig, Germany.

Institute of Biochemistry, Department of Chemistry & Center for Molecular Medicine, University of Cologne, Zülpicher Strasse 47, 50674 Cologne, Germany.

出版信息

Molecules. 2023 Oct 9;28(19):6998. doi: 10.3390/molecules28196998.

DOI:10.3390/molecules28196998
PMID:37836841
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC10574614/
Abstract

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.

摘要

亚硫酸氧化酶是真核生物中已知的五种含钼酶之一,它催化亚硫酸盐氧化为硫酸盐。这篇综述涵盖了亚硫酸氧化酶研究的历史,从其在脊椎动物中作为肝线粒体酶的早期发现开始,一直到激发了数十年研究的基本生化和结构特性。Ralf Mendel 提出了一种关于植物中亚硫酸氧化酶的个人观点,即硫酸盐被同化用于从头合成半胱氨酸,并介绍了这种定位于过氧化物体中单辅酶亚硫酸氧化酶的许多意外发现和独特性质。Guenter Schwarz 通过人类中亚硫酸氧化酶的缺乏将他的研究与之联系起来,证明了它在人类所有钼酶中的独特作用。从本质上讲,在植物和动物王国中,亚硫酸氧化酶都是氧化还原调节、信号转导和代谢中的重要参与者,从而以多种方式连接硫和氮代谢。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a9eb/10574614/049160598a50/molecules-28-06998-g009.jpg
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https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a9eb/10574614/36ffac047786/molecules-28-06998-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a9eb/10574614/c6345647bfc3/molecules-28-06998-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a9eb/10574614/1442740da4ef/molecules-28-06998-g008.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a9eb/10574614/049160598a50/molecules-28-06998-g009.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a9eb/10574614/ee28ecc40701/molecules-28-06998-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a9eb/10574614/4c7482752371/molecules-28-06998-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a9eb/10574614/4115a53b25a2/molecules-28-06998-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a9eb/10574614/9724f88da4a1/molecules-28-06998-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a9eb/10574614/d739a779a1a4/molecules-28-06998-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a9eb/10574614/36ffac047786/molecules-28-06998-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a9eb/10574614/c6345647bfc3/molecules-28-06998-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a9eb/10574614/1442740da4ef/molecules-28-06998-g008.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a9eb/10574614/049160598a50/molecules-28-06998-g009.jpg

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