Bryant, D.A., Hunter, C.N. orcid.org/0000-0003-2533-9783 and Warren, M.J. (2020) Biosynthesis of the modified tetrapyrroles—the pigments of life. Journal of Biological Chemistry, 295 (20). pp. 6888-6925. ISSN 0021-9258
Abstract
Modified tetrapyrroles are large macrocyclic compounds, consisting of diverse conjugation and metal chelation systems and imparting an array of colors to the biological structures that contain them. Tetrapyrroles represent some of the most complex small molecules synthesized by cells and are involved in many essential processes that are fundamental to life on Earth, including photosynthesis, respiration, and catalysis. These molecules are all derived from a common template through a series of enzyme-mediated transformations that alter the oxidation state of the macrocycle and also modify its size, its side-chain composition, and the nature of the centrally chelated metal ion. The different modified tetrapyrroles include chlorophylls, hemes, siroheme, corrins (including vitamin B12), coenzyme F430, heme d1, and bilins. After nearly a century of study, almost all of the more than 90 different enzymes that synthesize this family of compounds are now known, and expression of reconstructed operons in heterologous hosts has confirmed that most pathways are complete. Aside from the highly diverse nature of the chemical reactions catalyzed, an interesting aspect of comparative biochemistry is to see how different enzymes and even entire pathways have evolved to perform alternative chemical reactions to produce the same end products in the presence and absence of oxygen. Although there is still much to learn, our current understanding of tetrapyrrole biogenesis represents a remarkable biochemical milestone that is summarized in this review.
Metadata
Item Type: | Article |
---|---|
Authors/Creators: |
|
Copyright, Publisher and Additional Information: | © 2020 Bryant et al. Published by The American Society for Biochemistry and Molecular Biology, Inc. Final version open access under the terms of the Creative Commons CC-BY license. (http://creativecommons.org/licenses/by/4.0) |
Keywords: | heme; chlorophyll; biosynthesis; adenosylcobalamin (AdoCbl); photosynthesis; bacteriochlorophyll; bilin; tetrapyrrole; uroporphyrinogen III; vitamin B12; cobalamin; coenzyme F430; heme d1; 5-aminolevulinic acid; precorrin |
Dates: |
|
Institution: | The University of Sheffield |
Academic Units: | The University of Sheffield > Faculty of Science (Sheffield) > School of Biosciences (Sheffield) > Department of Molecular Biology and Biotechnology (Sheffield) |
Depositing User: | Symplectic Sheffield |
Date Deposited: | 02 Jun 2020 17:03 |
Last Modified: | 02 Jun 2020 17:03 |
Status: | Published |
Publisher: | American Society for Biochemistry & Molecular Biology (ASBMB) |
Refereed: | Yes |
Identification Number: | 10.1074/jbc.rev120.006194 |
Related URLs: | |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:161230 |