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古马亚斯湾热液喷口沉积物中的古烷菌可氧化石油烷烃。

Candidatus Alkanophaga archaea from Guaymas Basin hydrothermal vent sediment oxidize petroleum alkanes.

机构信息

Max Planck Institute for Marine Microbiology, Bremen, Germany.

MARUM, Center for Marine Environmental Sciences, University of Bremen, Bremen, Germany.

出版信息

Nat Microbiol. 2023 Jul;8(7):1199-1212. doi: 10.1038/s41564-023-01400-3. Epub 2023 Jun 1.

Abstract

Methanogenic and methanotrophic archaea produce and consume the greenhouse gas methane, respectively, using the reversible enzyme methyl-coenzyme M reductase (Mcr). Recently, Mcr variants that can activate multicarbon alkanes have been recovered from archaeal enrichment cultures. These enzymes, called alkyl-coenzyme M reductase (Acrs), are widespread in the environment but remain poorly understood. Here we produced anoxic cultures degrading mid-chain petroleum n-alkanes between pentane (C) and tetradecane (C) at 70 °C using oil-rich Guaymas Basin sediments. In these cultures, archaea of the genus Candidatus Alkanophaga activate the alkanes with Acrs and completely oxidize the alkyl groups to CO. Ca. Alkanophaga form a deep-branching sister clade to the methanotrophs ANME-1 and are closely related to the short-chain alkane oxidizers Ca. Syntrophoarchaeum. Incapable of sulfate reduction, Ca. Alkanophaga shuttle electrons released from alkane oxidation to the sulfate-reducing Ca. Thermodesulfobacterium syntrophicum. These syntrophic consortia are potential key players in petroleum degradation in heated oil reservoirs.

摘要

产甲烷菌和甲烷营养菌分别利用可逆转的酶甲基辅酶 M 还原酶(Mcr)来产生和消耗温室气体甲烷。最近,从古菌富集培养物中回收了可以激活多碳烷烃的 Mcr 变体。这些酶被称为烷基辅酶 M 还原酶(Acrs),在环境中广泛存在,但仍知之甚少。在这里,我们使用富含油的瓜伊马斯盆地沉积物,在 70°C 下培养缺氧培养物,降解中链石油正烷烃,范围从戊烷(C)到十四烷(C)。在这些培养物中,Candidatus Alkanophaga 属的古菌用 Acrs 激活烷烃,并将烷基完全氧化为 CO。Ca. Alkanophaga 与甲烷营养菌 ANME-1 形成一个深分支的姐妹分支,与短链烷烃氧化剂 Ca. Syntrophoarchaeum 密切相关。不能进行硫酸盐还原的 Ca. Alkanophaga 将从烷烃氧化释放的电子转移到硫酸盐还原的 Ca. Thermodesulfobacterium syntrophicum。这些共生联合体可能是加热油藏中石油降解的关键参与者。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6885/10322722/a9508c00c67c/41564_2023_1400_Fig1_HTML.jpg

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