Investigation of the prevalence and catalytic activity of rubredoxin-fused alkane monooxygenases (AlkBs).
AlkB
Alkane oxidation
Biocatalysis
Diiron enzymes
Monooxygenase
Rubredoxin
Journal
Journal of inorganic biochemistry
ISSN: 1873-3344
Titre abrégé: J Inorg Biochem
Pays: United States
ID NLM: 7905788
Informations de publication
Date de publication:
06 2021
06 2021
Historique:
received:
23
12
2020
revised:
28
01
2021
accepted:
21
02
2021
pubmed:
23
3
2021
medline:
18
1
2022
entrez:
22
3
2021
Statut:
ppublish
Résumé
Interest in understanding the environmental distribution of the alkane monooxygenase (AlkB) enzyme led to the identification of over 100 distinct alkane monooxygenase (AlkB) enzymes containing a covalently bound, or fused, rubredoxin. The rubredoxin-fused AlkB from Dietzia cinnamea was cloned as a full-length protein and as a truncated protein with the rubredoxin domain deleted. A point mutation (V91W) was introduced into the full-length protein, with the goal of assessing how steric bulk in the putative substrate channel might affect selectivity. Based on activity studies with alkane and alkene substrates, the rubredoxin-fused AlkB oxidizes a similar range of alkane substrates relative to its rubredoxin domain-deletion counterpart. Oxidation of terminal alkenes generated both an epoxide and a terminal aldehyde. The products of V91W-mutant-catalyzed oxidation of alkenes had a higher aldehyde-to-epoxide ratio than the products formed in the presence of the wild type protein. These results are consistent with this mutation causing a structural change impacting substrate positioning.
Identifiants
pubmed: 33752122
pii: S0162-0134(21)00056-8
doi: 10.1016/j.jinorgbio.2021.111409
pmc: PMC8557626
mid: NIHMS1687019
pii:
doi:
Substances chimiques
Alkanes
0
Alkenes
0
Bacterial Proteins
0
Rubredoxins
0
Mixed Function Oxygenases
EC 1.-
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
111409Subventions
Organisme : NIGMS NIH HHS
ID : R01 GM130989
Pays : United States
Informations de copyright
Copyright © 2021 Elsevier Inc. All rights reserved.
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