A novel alkane monooxygenase evolved from a broken piece of ribonucleotide reductase in Geobacillus kaustophilus HTA426 isolated from Mariana Trench.

IF 4.6 Q2 MATERIALS SCIENCE, BIOMATERIALS ACS Applied Bio Materials Pub Date : 2024-02-14 DOI:10.1007/s00792-024-01332-8
Tanasap Nithimethachoke, Chanita Boonmak, Masaaki Morikawa
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Abstract

We have accidentally found that a thermophilic Geobacillus kaustophilus HTA426 is capable of degrading alkanes although it has no alkane oxygenating enzyme genes. Our experimental results revealed that a putative ribonucleotide reductase small subunit GkR2loxI (GK2771) gene encodes a novel heterodinuclear Mn-Fe alkane monooxygenase/hydroxylase. GkR2loxI protein can perform two-electron oxidations similar to homonuclear diiron bacterial multicomponent soluble methane monooxygenases. This finding not only answers a long-standing question about the substrate of the R2lox protein clade, but also expands our understanding of the vast diversity and new evolutionary lineage of the bacterial alkane monooxygenase/hydroxylase family.

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从马里亚纳海沟分离的高嗜地气芽孢杆菌(Geobacillus kaustophilus HTA426)中的核糖核苷酸还原酶断片演化出一种新型烷烃单氧化酶。
我们意外地发现,嗜热革兰霉菌(Geobacillus kaustophilus)HTA426虽然没有烷烃加氧酶基因,却能够降解烷烃。我们的实验结果表明,推测的核糖核苷酸还原酶小亚基 GkR2loxI (GK2771) 基因编码一种新型异核锰铁烷烃单加氧酶/羟化酶。GkR2loxI 蛋白能进行类似于同核二铁细菌多组分可溶性甲烷单氧化酶的双电子氧化作用。这一发现不仅回答了有关R2lox蛋白族底物的一个长期存在的问题,而且拓展了我们对细菌烷烃单加氧酶/羟化酶家族的巨大多样性和新的进化脉络的认识。
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来源期刊
ACS Applied Bio Materials
ACS Applied Bio Materials Chemistry-Chemistry (all)
CiteScore
9.40
自引率
2.10%
发文量
464
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