Journal
JOURNAL OF INORGANIC BIOCHEMISTRY
Volume 219, Issue -, Pages -Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.jinorgbio.2021.111409
Keywords
Alkane oxidation; Monooxygenase; Diiron enzymes; AlkB; Rubredoxin; Biocatalysis
Funding
- National Institutes of Health [R01 GM130989]
- Presidential Research Fund at Barnard College
- Office of the Provost at Barnard
- Arnold and Mabel Beckman Foundation
- Evan B. Segal Grant Fund
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The research identified over 100 distinct alkane monooxygenase (AlkB) enzymes containing a covalently bound, or fused, rubredoxin. Mutations introduced into the enzymes affected their activity and substrate selectivity.
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 fulllength 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.
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