Structure and mechanism of the alkane-oxidizing enzyme AlkB.
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
17 04 2023
17 04 2023
Historique:
received:
23
03
2023
accepted:
03
04
2023
medline:
19
4
2023
entrez:
17
4
2023
pubmed:
18
4
2023
Statut:
epublish
Résumé
Alkanes are the most energy-rich form of carbon and are widely dispersed in the environment. Their transformation by microbes represents a key step in the global carbon cycle. Alkane monooxygenase (AlkB), a membrane-spanning metalloenzyme, converts straight chain alkanes to alcohols in the first step of the microbially-mediated degradation of alkanes, thereby playing a critical role in the global cycling of carbon and the bioremediation of oil. AlkB biodiversity is attributed to its ability to oxidize alkanes of various chain lengths, while individual AlkBs target a relatively narrow range. Mechanisms of substrate selectivity and catalytic activity remain elusive. Here we report the cryo-EM structure of AlkB, which provides a distinct architecture for membrane enzymes. Our structure and functional studies reveal an unexpected diiron center configuration and identify molecular determinants for substrate selectivity. These findings provide insight into the catalytic mechanism of AlkB and shed light on its function in alkane-degrading microorganisms.
Identifiants
pubmed: 37069165
doi: 10.1038/s41467-023-37869-z
pii: 10.1038/s41467-023-37869-z
pmc: PMC10110569
doi:
Substances chimiques
Alkanes
0
Carbon
7440-44-0
AlkB Enzymes
EC 1.14.11.33
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Sous-ensembles de citation
IM
Pagination
2180Subventions
Organisme : NIGMS NIH HHS
ID : R01 GM130989
Pays : United States
Organisme : NIGMS NIH HHS
ID : U24 GM129541
Pays : United States
Informations de copyright
© 2023. The Author(s).
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