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The Role of Dioxygen in Microbial Biocatalysis and Biodegradation – Challenging Biochemistry, Illustrated by a Short History of a Long Misunderstood Enzyme
Version 1
: Received: 2 January 2024 / Approved: 4 January 2024 / Online: 4 January 2024 (07:12:14 CET)
How to cite:
Willetts, A. The Role of Dioxygen in Microbial Biocatalysis and Biodegradation – Challenging Biochemistry, Illustrated by a Short History of a Long Misunderstood Enzyme. Preprints2024, 2024010312. https://doi.org/10.20944/preprints202401.0312.v1
Willetts, A. The Role of Dioxygen in Microbial Biocatalysis and Biodegradation – Challenging Biochemistry, Illustrated by a Short History of a Long Misunderstood Enzyme. Preprints 2024, 2024010312. https://doi.org/10.20944/preprints202401.0312.v1
Willetts, A. The Role of Dioxygen in Microbial Biocatalysis and Biodegradation – Challenging Biochemistry, Illustrated by a Short History of a Long Misunderstood Enzyme. Preprints2024, 2024010312. https://doi.org/10.20944/preprints202401.0312.v1
APA Style
Willetts, A. (2024). The Role of Dioxygen in Microbial Biocatalysis and Biodegradation – Challenging Biochemistry, Illustrated by a Short History of a Long Misunderstood Enzyme. Preprints. https://doi.org/10.20944/preprints202401.0312.v1
Chicago/Turabian Style
Willetts, A. 2024 "The Role of Dioxygen in Microbial Biocatalysis and Biodegradation – Challenging Biochemistry, Illustrated by a Short History of a Long Misunderstood Enzyme" Preprints. https://doi.org/10.20944/preprints202401.0312.v1
Abstract
a Special Issue of Microorganisms devoted to ‘Microbial Biocatalysis and Biodegradation’ would be incomplete without some form of acknowledgement of the many important roles that dioxygen-dependent enzymes (principally mono- and dioxygenases) play in relevant aspects of biooxygenation. This is reflected by the multiple strategic roles that dioxygen-dependent microbial enzymes play both in generating valuable synthons for chemoenzymatic synthesis, and in facilitating key reactions that drive the global geochemical Carbon Cycle. A useful insight into this relationship can be gained by reviewing the evolution of the current status of 2,5-diketocamphane 1,2-monooxygenase (EC 1.14.14.108) from camphor-grown Pseudomonas putida ATCC 17453. Over the last sixty years, the perceived nature of this monooxygenase has transmogrified significantly. Commencing in the 1960s, extensive initial studies consistently reported that the enzyme was a monomeric true flavoprotein dependent on both FMNH2 and nonheme iron as bound cofactors. However, over the last decade all those criteria have changed absolutely, and the enzyme is currently acknowledged to be a metal ion-independent homodimeric flavin-dependent two-component monooxygenase deploying FMNH2 as a cosubstrate. That transition is a paradigm of the ever evolving nature of scientific knowledge.
Biology and Life Sciences, Biochemistry and Molecular Biology
Copyright:
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
