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细菌中通过粪卟啉依赖性途径对血红素生物合成的调控。

Regulation of heme biosynthesis via the coproporphyrin dependent pathway in bacteria.

作者信息

Aftab Hadia, Donegan Rebecca K

机构信息

Department of Chemistry, Barnard College, New York, NY, United States.

出版信息

Front Microbiol. 2024 Mar 21;15:1345389. doi: 10.3389/fmicb.2024.1345389. eCollection 2024.

DOI:10.3389/fmicb.2024.1345389
PMID:38577681
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC10991733/
Abstract

Heme biosynthesis in the Gram-positive bacteria occurs mostly via a pathway that is distinct from that of eukaryotes and Gram-negative bacteria in the three terminal heme synthesis steps. In many of these bacteria heme is a necessary cofactor that fulfills roles in respiration, gas sensing, and detoxification of reactive oxygen species. These varying roles for heme, the requirement of iron and glutamate, as glutamyl tRNA, for synthesis, and the sharing of intermediates with the synthesis of other porphyrin derivatives necessitates the need for many points of regulation in response to nutrient availability and metabolic state. In this review we examine the regulation of heme biosynthesis in these bacteria via heme, iron, and oxygen species. We also discuss our perspective on emerging roles of protein-protein interactions and post-translational modifications in regulating heme biosynthesis.

摘要

革兰氏阳性菌中的血红素生物合成大多通过一条途径进行,该途径在血红素合成的三个末端步骤中与真核生物和革兰氏阴性菌的途径不同。在许多这类细菌中,血红素是一种必需的辅因子,在呼吸作用、气体传感和活性氧解毒中发挥作用。血红素的这些不同作用、合成过程中对铁和作为谷氨酰tRNA的谷氨酸的需求,以及与其他卟啉衍生物合成过程中中间体的共享,使得需要根据营养物质的可利用性和代谢状态进行多个调控点的调节。在本综述中,我们研究了这些细菌中通过血红素、铁和氧物种对血红素生物合成的调控。我们还讨论了我们对蛋白质-蛋白质相互作用和翻译后修饰在调控血红素生物合成中的新作用的看法。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fcea/10991733/12f6adb6fac6/fmicb-15-1345389-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fcea/10991733/6685707c7c88/fmicb-15-1345389-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fcea/10991733/4506294c99af/fmicb-15-1345389-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fcea/10991733/12f6adb6fac6/fmicb-15-1345389-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fcea/10991733/6685707c7c88/fmicb-15-1345389-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fcea/10991733/4506294c99af/fmicb-15-1345389-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fcea/10991733/12f6adb6fac6/fmicb-15-1345389-g003.jpg

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Biology (Basel). 2023 Dec 15;12(12):1527. doi: 10.3390/biology12121527.
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Biomolecules. 2023 Oct 6;13(10):1485. doi: 10.3390/biom13101485.
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Iron insertion into coproporphyrin III-ferrochelatase complex: Evidence for an intermediate distorted catalytic species.
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