DOCSLIB.ORG

Downloaded from 5Quadram Institute Bioscience, Norwich Research Park, Norwich NR4 7UQ, United Kingdom

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
Downloaded from 5Quadram Institute Bioscience, Norwich Research Park, Norwich NR4 7UQ, United Kingdom Kent Academic Repository Full text document (pdf) Citation for published version Bryant, Donald A. and Hunter, C. Neil and Warren, Martin J. (2020) Biosynthesis of the modified tetrapyrroles: the pigments of life. Journal of Biological Chemistry . ISSN 0021-9258. DOI https://doi.org/10.1074/jbc.REV120.006194 Link to record in KAR https://kar.kent.ac.uk/80865/ Document Version Author's Accepted Manuscript Copyright & reuse Content in the Kent Academic Repository is made available for research purposes. Unless otherwise stated all content is protected by copyright and in the absence of an open licence (eg Creative Commons), permissions for further reuse of content should be sought from the publisher, author or other copyright holder. Versions of research The version in the Kent Academic Repository may differ from the final published version. Users are advised to check http://kar.kent.ac.uk for the status of the paper. Users should always cite the published version of record. Enquiries For any further enquiries regarding the licence status of this document, please contact: [email protected] If you believe this document infringes copyright then please contact the KAR admin team with the take-down information provided at http://kar.kent.ac.uk/contact.html JBC Papers in Press. Published on April 2, 2020 as Manuscript REV120.006194 The latest version is at https://www.jbc.org/cgi/doi/10.1074/jbc.REV120.006194 Biosynthesis of the modified tetrapyrroles—the pigments of life Donald A. Bryant1,2*, C. Neil Hunter3,‡, and Martin J. Warren4,5,§ 1Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA 16802 2Department of Chemistry and Biochemistry, Montana State University, Bozeman, MT 59717 3Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield S10 2TN, United Kingdom 4School of Biosciences, University of Kent, Canterbury, CT2 7NJ, United Kingdom Downloaded from 5Quadram Institute Bioscience, Norwich Research Park, Norwich NR4 7UQ, United Kingdom. http://www.jbc.org/ *Corresponding author: Donald A. Bryant E-mail: [email protected] by guest on April 14, 2020 ‡Corresponding author: C. Neil Hunter E-mail: [email protected] §Corresponding author: Martin J. Warren E-mail: [email protected] Running Title: Biosynthesis of modified tetrapyrroles Key Words: heme; chlorophyll, bilin; vitamin B12; cobalamin, coenzyme F430; heme d1; biosynthesis; tetrapyrrole; 5-aminolevulinic acid; uroporphyrinogen III; precorrin. 1 Abstract dubbed the “pigments of life” (1). These life pigments include the hemes, Modified tetrapyrroles are large chlorophylls (Chls), bilins, corrins (vitamin macrocyclic compounds, consisting of B12), siroheme, and coenzyme F430. They diverse conjugation and metal chelation are all made from a single, extensively systems and imparting an array of colors to branched biosynthetic pathway and are the biological structures that contain them. based on the blueprint of a common Tetrapyrroles represent some of the most biosynthetic primogenitor, complex small molecules synthesized by uroporphyrinogen III (Fig. 1). These cells and are involved in many essential different modified tetrapyrroles vary in the processes that are fundamental to life on nature of their peripheral side chains, the Earth, including photosynthesis, oxidation state of the macrocycle itself and respiration, and catalysis. These molecules the centrally chelated metal ion. Perhaps the are all derived from a common template most distinctive of all is vitamin B12, which through a series of enzyme-mediated contains a ring-contracted macrocycle and transformations that alter the oxidation state also houses upper and lower ligands in of the macrocycle, and also modify its size, order to provide the octahedral geometry to side chain composition, and the nature of coordinate the cobalt ion. Downloaded from the centrally chelated metal ion. The The differences in the structures of different modified tetrapyrroles include these molecules are reflected in diverse chlorophylls, hemes, siroheme, corrins biological functions. Some of the modified (including vitamin B12), coenzyme F430, tetrapyrroles are involved in very specific http://www.jbc.org/ heme d1 and bilins. After nearly a century processes; for example heme d is required of study, almost all of the more than 90 1 as a prosthetic group only for the cd1 nitrite different enzymes that synthesize this reductase (2), whereas others, such as family of compounds are now known, and heme, are involved in a myriad of distinct expression of reconstructed operons in biological roles, from sensing to catalysis by guest on April 14, 2020 heterologous hosts has confirmed that most (3). A brief description of the roles played pathways are complete. Aside from the by these molecules is outlined below. highly diverse nature of the chemical reactions catalyzed, an interesting aspect of Chls and the related comparative biochemistry is to see how bacteriochlorophylls (BChls) are the different enzymes and even entire pathways molecules that not only give plants their have evolved to perform alternative green pigmentation but are intricately chemical reactions to produce the same end involved in the process of photosynthesis products in the presence and absence of (4). Chls play two roles in photosynthesis: oxygen. Although there is still much to firstly, they act as antenna molecules and learn, our current understanding of harvest solar energy; and secondly, they tetrapyrrole biogenesis represents a transfer this energy to the reaction centers, remarkable biochemical milestone that is where photochemistry occurs that results in summarized in this review. the splitting of water or the production of strong reductants for carbon dioxide fixation and ATP generation. With only a Introduction few exceptions in which Zn2+ replaces Modified tetrapyrroles play essential roles Mg2+, Chls are Mg2+-containing chlorins, in a broad range of essential biological and the electronic properties of the chlorin processes. Their large macrocyclic ring allow for the efficient formation of a structures and diverse conjugation and singlet excited state upon visible light metal chelation systems also provide an absorption. In contrast to the metal ions array of colors such that they have been found in other modified tetrapyrroles, Mg2+ 2 is not redox active and the metal does not homolytic cleavage of the Co-adenosyl play a direct role in the light-trapping bond. These reactions include, among many process. However, the metal does appear to others, methylmalonyl CoA mutase, help potentiate the chemistry of the chlorin ribonucleotide reductase and the diol ring to make energy transfer more efficient. dehydratases (7). Adenosylcobalamin has also recently been shown to be involved as Heme is technically an Fe-containing a light sensor in a transcription factor (8). porphyrin. It has one more double bond in Corrinoids without an upper ligand act as the macrocycle than Chls and the extra the catalytic center for reductive conjugation helps produce the red colour dehalogenases, in which the cobalt ion is associated with the molecule. The central thought to form a direct bond with the Fe ion is crucial to the functions for which halide component of the substrate in order heme is used (5). Iron exists in several to mediate its abstraction (9). Finally, both oxidation states and, for this reason, heme methylcorrinoids and adenosylcorrinoids has evolved a broad range of roles within also appear to be involved in a specific biological systems, from acting as a one- group of radical SAM enzymes (6); B electron carrier in respiratory cytochromes 12- to a sensing role for a range of diatomic radical SAM enzymes are the largest group within this broad enzyme class (10). Downloaded from gases including CO, NO and O2. Heme also acts as the prosthetic group in a range of Coenzyme F430 is a nickel-containing enzymes including catalases, peroxidases tetrahydroporphyrinogen and acts as a and cytochromes P450, and is known to be coenzyme in both forward and reverse associated with certain transporters and methanogenesis (11). As a coenzyme http://www.jbc.org/ transcription factors (3). within coenzyme M reductase, the central nickel ion is able to mediate the reversible The corrinoids, sometimes also reduction/oxidation of a methyl group to referred to as cobamides, encompass produce methane in both the processes of cofactors and coenzymes that harbor by guest on April 14, 2020 methanogenesis and anaerobic methane cobalt-containing, ring-contracted corrin oxidation. In some respects, the binding of macrocycles. In biologically active nickel in coenzyme F corrinoids the cobalt atom is covalently 430 mirrors the binding linked to either a methyl or adenosyl group of cobalt in corrins, reflecting similarities in on the upper face of the macrocycle. The their respective catalytic activities in corrin ring is also attached to a lower forming metal-carbon bonds. However, in nucleotide loop via one of its propionate coenzyme F430, nickel promotes methyl side chains. The nature of the base in this group reduction, whilst in corrinoid- nucleotide loop varies among bacteria, and dependent methyltransferases the cobalt over 20 different bases are known to be promotes methyl group transfer (12). incorporated into corrinoids. The base is Demonstrating the importance of these specifically dimethylbenzimidazole in tetrapyrrole catalysts, the process of methanogenesis is responsible for the vitamin B
Load more

Recommended publications
  • 192ICM ICBIC Posters
    Journal of Inorganic Biochemistry 96 (2003) 203 Monomeric TpPrMoVOSR complexes via the chemical reduction of TpPrMoVIOSR. David J Nielsen, School of Chemistry, University of Melbourne, Australia Christian J Doonan, School of Chemistry, University of Melbourne, Australia Graham N George, Stanford Synchrotron Radiation Laboratory, United States Hugh Harris, Stanford Synchrotron Radiation Laboratory, United States Charles G Young, University of Melbourne, Australia EPR evidence has suggested the presence of molybdenum(V) intermediates in the catalytic cycle of hydroxylase enzyme systems [1], and references therein], and as such these species are attractive targets for the synthesis of small-molecule model systems. Ongoing work in our group has allowed access to several stable and well characterised monomeric molybdenum(VI) oxo-thio complexes TpPrMoVIOSR (TpPr = hydridotris(3-isopropylpyrazol-1-yl)borate) with co-ligand R = eg. substituted phenolates [2], as shown below. These Mo(VI) complexes have proved amenable to chemical reduction using cobaltocene (CoCp2) yielding initially the Pr V [CoCp2][Tp Mo OSR] salts [1,2]. Solution and solid state sulfur X-ray absorption spectroscopy (XAS) on selected examples of the chemically reduced species shows pre-edge features attributable to the S 1s → Mo=S π* transition of a [MoOS]+ unit. Further spectroscopic investigations (EPR, IR) are consistent with the presence of a paramagnetic Mo(V) centre bearing a terminal thio ligand. Continuing spectroscopic, structural and reactivity investigations centred on these important species will be presented. References: [1] P. D. Smith, D. A. Slizys, G. N. George and C. G. Young, J. Amer. Chem. Soc., 122(12), 2000, 2946. [2] C. J. Doonan, Unpublished results.
    [Show full text]
  • Van Heuvelen Department of Chemistry, Harvey Mudd College
    Development of Bio-Inspired Catalysts for Dechlorination Reactions Prof. Katherine Van Heuvelen Department of Chemistry, Harvey Mudd College Abstract The nickel-containing cofactor F430 found in methyl-coenzyme M reductase (MCR) and the cobalt-containing cobalamin cofactor (Cbl) found in Vitamin B12 carry out the reductive dehalogenation of chlorinated alkenes, which can act as damaging pollutants in the environment. Both F430 and Cbl are found in biological systems and carry out this reaction under benign conditions using earth-abundant materials. This work centers on the preparation and investigation of small molecular model compounds that reproduce key geometric and electronic features of cofactors F430 and Cbl. In particular, I propose to: 1. Prepare a series of nickel- and cobalt-containing F430 model compounds designed to investigate the influence of the supporting ligand on reactivity. 2. Evaluate the reactivity of these complexes towards halogenated substrates. 3. Characterize reaction intermediates using a combination of spectroscopic (UV-visible, infrared, NMR) and computational (density functional theory, DFT) techniques in order to correlate geometric and electronic structure with reactivity. 4. Elucidate the reaction mechanism using insights gained from aims 1–3, ultimately applying a detailed understanding of the fundamental chemistry underlying dehalogenation to the rational design of an improved catalytic system to treat chlorinated pollutants before they enter the water supply. Start Date, Duration, and Location This research will be conducted at Harvey Mudd College over a ten-week period in the summer of 2016, which will run from May 23 – July 29. The Chemistry Department is in the process of hiring students for the summer of 2016 and the student working on this project will be identified later in the spring semester.
    [Show full text]
  • Deciphering the Mechanism of Enzymatic Methane Synthesis
    Science Highlight – June 2021 Deciphering the Mechanism of Enzymatic Methane Synthesis Methane is the simplest organic compound with the highest energy content of any carbon- based fuel. Methane accounts for almost a quarter of U.S. energy consumption, with one-half of homes using natural gas as their heating fuel.1-2 Interestingly, more than 90% of all methane on earth is produced biogenically by methanogens which are responsible for enzymatic synthesis of 1 billion tons of methane per year.3-4 Much of the methane formed by methanogens is captured and used as an energy source by aerobic and anaerobic methanotrophic microbes.5-6 However, the increased mining of methane and industrial farming of cattle has created a mismatch between the sources and the sinks of methane, causing its atmospheric levels to double over the past two centuries. This is an environmental concern related to climate change because pound for pound, methane causes 25 times more 7 global warming over a 100-year period than CO2. Thus, understanding the biosynthesis of methane is imperative from basic energy, economic and environmental perspectives. Methane is formed by one of the few Ni containing cofactors (F430) as part of the active site of methyl coenzyme M reductase (MCR), a strictly anaerobic enzyme present in methanogenic archaea. MCR catalyzes the reaction of methyl-coenzyme M (CH3−SCoM) with coenzyme B (HSCoB) to form methane and the heterodisulfide CoMS−SCoB.8 Besides the importance of methane metabolism in our environment and global energy landscape, the basic chemistry and biology of alkane activation and formation by MCR are of fundamental interest.
    [Show full text]
  • Characterisation, Classification and Conformational Variability Of
    Characterisation, Classification and Conformational Variability of Organic Enzyme Cofactors Julia D. Fischer European Bioinformatics Institute Clare Hall College University of Cambridge A thesis submitted for the degree of Doctor of Philosophy 11 April 2011 This dissertation is the result of my own work and includes nothing which is the outcome of work done in collaboration except where specifically indicated in the text. This dissertation does not exceed the word limit of 60,000 words. Acknowledgements I would like to thank all the members of the Thornton research group for their constant interest in my work, their continuous willingness to answer my academic questions, and for their company during my time at the EBI. This includes Saumya Kumar, Sergio Martinez Cuesta, Matthias Ziehm, Dr. Daniela Wieser, Dr. Xun Li, Dr. Irene Pa- patheodorou, Dr. Pedro Ballester, Dr. Abdullah Kahraman, Dr. Rafael Najmanovich, Dr. Tjaart de Beer, Dr. Syed Asad Rahman, Dr. Nicholas Furnham, Dr. Roman Laskowski and Dr. Gemma Holli- day. Special thanks to Asad for allowing me to use early development versions of his SMSD software and for help and advice with the KEGG API installation, to Roman for knowing where to find all kinds of data, to Dani for help with R scripts, to Nick for letting me use his E.C. tree program, to Tjaart for python advice and especially to Gemma for her constant advice and feedback on my work in all aspects, in particular the chemistry side. Most importantly, I would like to thank Prof. Janet Thornton for giving me the chance to work on this project, for all the time she spent in meetings with me and reading my work, for sharing her seemingly limitless knowledge and enthusiasm about the fascinating world of enzymes, and for being such an experienced and motivational advisor.
    [Show full text]
  • Downloaded from the Genome NCBI
    bioRxiv1 preprint doi: https://doi.org/10.1101/765248; this version posted July 16, 2020. The copyright holder for this preprint (which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission. 1 Groundwater Elusimicrobia are metabolically diverse compared to gut microbiome Elusimicrobia 2 and some have a novel nitrogenase paralog. 3 4 Raphaël Méheust1,2, Cindy J. Castelle1,2, Paula B. Matheus Carnevali1,2, Ibrahim F. Farag3, Christine He1, 5 Lin-Xing Chen1,2, Yuki Amano4, Laura A. Hug5, and Jillian F. Banfield1,2,*. 6 7 1Department of Earth and Planetary Science, University of California, Berkeley, Berkeley, CA 94720, 8 USA 9 2Innovative Genomics Institute, Berkeley, CA 94720, USA 10 3School of Marine Science and Policy, University of Delaware, Lewes, DE 19968, USA 11 4Nuclear Fuel Cycle Engineering Laboratories, Japan Atomic Energy Agency, Tokai-mura, Ibaraki, Japan 12 5Department of Biology, University of Waterloo, ON, Canada 13 *Corresponding author: Email: [email protected] 14 15 Abstract 16 Currently described members of Elusimicrobia, a relatively recently defined phylum, are animal- 17 associated and rely on fermentation. However, free-living Elusimicrobia have been detected in sediments, 18 soils and groundwater, raising questions regarding their metabolic capacities and evolutionary 19 relationship to animal-associated species. Here, we analyzed 94 draft-quality, non-redundant genomes, 20 including 30 newly reconstructed genomes, from diverse animal-associated and natural environments. 21 Genomes group into 12 clades, 10 of which previously lacked reference genomes. Groundwater- 22 associated Elusimicrobia are predicted to be capable of heterotrophic or autotrophic lifestyles, reliant on 23 oxygen or nitrate/nitrite-dependent respiration, or a variety of organic compounds and Rhodobacter 24 nitrogen fixation-dependent (Rnf-dependent) acetogenesis with hydrogen and carbon dioxide as the 25 substrates.
    [Show full text]
  • Methane Generation Via Intraprotein C-S Bond Cleavage in Cytochrome
    Journal of Organometallic Chemistry 901 (2019) 120945 Contents lists available at ScienceDirect Journal of Organometallic Chemistry journal homepage: www.elsevier.com/locate/jorganchem Methane generation via intraprotein CeS bond cleavage in cytochrome b562 reconstituted with nickel didehydrocorrin * ** Yuta Miyazaki a, Koji Oohora a, b, , Takashi Hayashi a, a Department of Applied Chemistry, Graduate School of Engineering, Osaka University, Suita, 565-0871, Japan b Frontier Research Base for Global Young Researchers, Graduate School of Engineering, Osaka University, Suita, 565-0871, Japan article info abstract II Article history: Cytochrome b562 (Cyt b562) reconstituted with nickel didehydrocorrin (Ni (DDHC)), a protein-based Received 20 August 2019 functional model of methyl-coenzyme M reductase (MCR), was investigated to demonstrate methane Received in revised form generation via intraprotein cleavage of a CeS bond. NiII(DDHC) was synthesized as a model complex of an 16 September 2019 MCR cofactor known as F430 and found to show NiII/NiI redox behavior with a potential of À0.61 V vs. Accepted 18 September 2019 AgjAgCl. This potential is slightly positive-shifted compared to that of F430 without protein. Conjugation Available online 19 September 2019 II II of Ni (DDHC) with the apo-form of Cyt b562 provides reconstituted Cyt b562 (rCyt b562(Ni (DDHC))) which II was characterized by spectroscopic measurements. Photoirradiation of rCyt b562(Ni (DDHC)) generates Keywords: 0 Hemoprotein methane gas in the presence of tris(2,2 -bipyridine)ruthenium(II) chloride as a photosensitizer and so- fi MCR dium ascorbate as a sacri cial reagent. Further experiments using Cyt b562 mutants indicate that F430 methane is derived from the CH3S group of the methionine residue in the heme-binding site where Methane thioether, thiol and the nickel center are precisely arranged.
    [Show full text]
  • A Niii-Containing Vitamin B12 Derivative with a Cofactor-F430
    Zurich Open Repository and Archive University of Zurich Main Library Strickhofstrasse 39 CH-8057 Zurich www.zora.uzh.ch Year: 2018 A Nickel(II)-Containing Vitamin B12 Derivative with a Cofactor-F430-type ฀-System Brenig, Christopher ; Prieto, Lucas ; Oetterli, René ; Zelder, Felix Abstract: F430 is a unique enzymatic cofactor in the production and oxidation of methane by strictly anaerobic bacteria. The key enzyme methyl coenzyme M reductase (MCR) contains a hydroporphi- noid nickel complex with a characteristic absorption maximum at around 430 nm in its active site. Herein, the three‐step semisynthesis of a hybrid NiII‐containing corrinoid that partly resembles F430 in its structural and spectroscopic features from vitamin B12 is presented. A key step of the route is the simultaneous demetalation and ring closure reaction of a 5,6‐secocobalamin to metal‐free 5,6‐dihy- droxy‐5,6‐dihydrohydrogenobalamin with cobaltocene and KCN under reductive conditions. Studies on the coordination chemistry of the novel compound support an earlier hypothesis why nature carefully selected a corphin over a corrin ligand in F430 for challenging nickel‐catalyzed biochemical reactions. DOI: https://doi.org/10.1002/anie.201810983 Posted at the Zurich Open Repository and Archive, University of Zurich ZORA URL: https://doi.org/10.5167/uzh-183474 Journal Article Accepted Version Originally published at: Brenig, Christopher; Prieto, Lucas; Oetterli, René; Zelder, Felix (2018). A Nickel(II)-Containing Vita- min B12 Derivative with a Cofactor-F430-type ฀-System. Angewandte Chemie Internationale Edition, 57(50):16308-16312. DOI: https://doi.org/10.1002/anie.201810983 II A Ni -Containing Vitamin B12 Derivative with a Cofactor-F430-Type π-System Christopher Brenig‡, Lucas Prieto‡, René Oetterli and Felix Zelder* Department of Chemistry, University of Zurich, Winterthurerstrasse 190, CH-8057 Zurich, Switzerland.
    [Show full text]
  • Publications R. Thauer Publications of RK Thauer
    Publications R. Thauer Publications of R. K. Thauer (42 pages) (04-06-18) Web of Science: h = 79 (almost 26,000 citations) Google Scholar: h = 93 (over 36,000 citations) Page Theses (3) 1 Original Publications (349) 1 Reviews (76) 32 Published lectures (38) 38 Miscellaneous (19) 42 Theses (3) Thauer, R.K. (1966) Protein-Biosynthese in Ehrlichs-Ascites-Tumor-Zellen unter der Einwirkung von Natulan. Diplomarbeit, Universität Tübingen. Thauer, R.K. (1968) Der Energiestoffwechsel von Clostridium kluyveri. Dissertation, Universität Freiburg. Thauer, R.K. (1971) Biochemie und Physiologie von vier neuen Ferredoxin- abhängigen Reaktionen. Habilitationsschrift, Universität Freiburg Original Publications (349) Tübingen Thauer, R.K., Stöffler, G. und Uehleke, H. (1965) N-Hydroxylierung von Sulfanilamid zu p-Hydroxylamiobenzolsulfonamid durch Lebermikrosomen. Naunyn-Schmiedebergs Arch. exp. Path. u. Pharmak. 252, 32-42. Thauer, R.K., Meiforth, A. und Uehleke, H. (1965) Methämoglobinbildung durch Sulfonamide im System Leberhomogenat, Erythrocyten, NADPH und Sauerstoff. Naunyn-Schmiedebergs Arch. exp. Path. u. Pharmak. 252, 291- 296. Stöffler, G., Thauer, R.K. und Uehleke, H. (1966) Methämglobinbildung durch p-Hydroxylamino- und p-Nitrosobenzolsulfonamid in Nabelschnur und Erwachsenen-Erythrocyten. Naunyn-Schmiedebergs Arch. exp. Path. u. Pharmak. 252, 359-367. Weitzel, G., Schneider, F., Hirschmann, W.D., Durst, J., Thauer, R.K., Ochs, H. und Kummer, D. (1967) Untersuchungen zum cytostatischen Wirkungsmechanismus der Methylhydrazine, III. Hoppe Seyler's Z. Physiol. Chem. 348, 443-454 1 Original Publications R. Thauer Freiburg Decker, K., Thauer, R.K. und Jungermann, K. (1966) Die Kohlenhydratsynthese in Clostridium kluyveri. I. Isotopenversuche zur Biosynthese der Ribose. Biochem. Z. 345, 461-471. Decker, K., Jungermann, K., Thauer, R.K.
    [Show full text]
  • Chlorophylls, Symmetry, Chirality, and Photosynthesis †,‡
    Symmetry 2014, 6, 781-843; doi:10.3390/sym6030781 OPEN ACCESS symmetry ISSN 2073-8994 www.mdpi.com/journal/symmetry Review Chlorophylls, Symmetry, Chirality, and Photosynthesis †,‡ Mathias O. Senge 1,2,*, Aoife A. Ryan 1, Kristie A. Letchford 1, Stuart A. MacGowan 1 and Tamara Mielke 1 1 SFI Tetrapyrrole Laboratory, Trinity Biomedical Sciences Institute, School of Chemistry, 152-160 Pearse Street, Trinity College Dublin, The University of Dublin, Dublin 2, Ireland; E-Mails: [email protected] (A.A.R.); [email protected] (K.A.L.); [email protected] (S.A.M.); [email protected] (T.M.) 2 Institute of Molecular Medicine, Medicinal Chemistry, Trinity Centre for Health Sciences, Trinity College Dublin, St. James’s Hospital, Dublin 8, Ireland † Structure and Conformation of Photosynthetic Pigments and Related Compounds. Part 14. ‡ Dedicated to Professor Horst Senger. * Author to whom correspondence should be addressed; E-Mail: [email protected]; Tel.: +353-896-8537; Fax: +353-896-8536. Received: 28 July 2014; in revised form: 31 August 2014 / Accepted: 1 September 2014 / Published: 10 September 2014 Abstract: Chlorophylls are a fundamental class of tetrapyrroles and function as the central reaction center, accessory and photoprotective pigments in photosynthesis. Their unique individual photochemical properties are a consequence of the tetrapyrrole macrocycle, the structural chemistry and coordination behavior of the phytochlorin system, and specific substituent pattern. They achieve their full potential in solar energy conversion by working in concert in highly complex, supramolecular structures such as the reaction centers and light-harvesting complexes of photobiology. The biochemical function of these structures depends on the controlled interplay of structural and functional principles of the apoprotein and pigment cofactors.
    [Show full text]
  • Studies of the Distinguishing Features of NADPH:2-Ketopropyl-Coenzyme
    Utah State University DigitalCommons@USU All Graduate Theses and Dissertations Graduate Studies 8-2011 Studies of the Distinguishing Features of NADPH:2-Ketopropyl- Coenzyme M Oxidoreductase/Carboxylase, an Atypical Member of the Disulfide/ Oxidoreductase Family of Enzymes Melissa A. Beighley-Kofoed Utah State University Follow this and additional works at: https://digitalcommons.usu.edu/etd Part of the Biochemistry, Biophysics, and Structural Biology Commons Recommended Citation Beighley-Kofoed, Melissa A., "Studies of the Distinguishing Features of NADPH:2-Ketopropyl-Coenzyme M Oxidoreductase/Carboxylase, an Atypical Member of the Disulfide/ Oxidoreductase Family of Enzymes" (2011). All Graduate Theses and Dissertations. 1012. https://digitalcommons.usu.edu/etd/1012 This Dissertation is brought to you for free and open access by the Graduate Studies at DigitalCommons@USU. It has been accepted for inclusion in All Graduate Theses and Dissertations by an authorized administrator of DigitalCommons@USU. For more information, please contact [email protected]. STUDIES OF THE DISTINGUISHING FEATURES OF NADPH:2-KETOPROPYL- COENZYME M OXIDOREDUCTASE/CARBOXYLASE, AN ATYPICAL MEMBER OF THE DISULFIDE OXIDOREDUCTASE FAMILY OF ENZYMES by Melissa Kofoed A dissertation submitted in partial fulfillment of the requirements for the degree of DOCTOR OF PHILOSOPHY in Biochemistry Approved: ______________________________ ______________________________ Scott A. Ensign, Ph.D. Lance C. Seefeldt, Ph.D. Major Professor Committee Member ______________________________ ______________________________ Joan M. Hevel, Ph.D. John L. Hubbard, Ph.D. Committee Member Committee Member ______________________________ ______________________________ Paul G. Wolf, Ph.D. Mark R. McLellan, Ph.D. Committee Member Vice President for Research and Dean of Graduate Studies and UTAH STATE UNIVERSITY Logan, Utah 2011 ii Copyright © Melissa A.
    [Show full text]
  • Chemical Communications FEATURE
    Chemical Communications FEATURE Conformational control of cofactors in nature – The influence of protein‐induced macrocycle distortion on the biological function Received 00th January 20xx, Accepted 00th January 20xx of tetrapyrroles a,b* a b DOI: 10.1039/c5cc06254c Mathias O. Senge, Stuart A. MacGowan and Jessica O’Brien www.rsc.org/ Tetrapyrrole‐containing proteins are one of the most fundamental classes of enzymes in nature and it remains an open question to give a chemical rationale for the multitude of biological reactions that can be catalyzed by these pigment‐ protein complexes. There are many fundamental processes where the same (i.e., chemically identical) porphyrin cofactor is involved in chemically quite distinct reactions. For example, heme is the active cofactor for oxygen transport and storage (hemoglobin, myoglobin) and for the incorporation of molecular oxygen in organic substrates (cytochrome P450). It is involved in the terminal oxidation (cytochrome c oxidase) and the metabolism of H2O2 (catalases and peroxidases) and catalyzes various electron transfer reactions in cytochromes. Likewise, in photosynthesis the same chlorophyll cofactor may function as a reaction center pigment (charge separation) or as an accessory pigment (exciton transfer) in light harvesting complexes (e.g., chlorophyll a). Whilst differences in the apoprotein sequences alone cannot explain the often drastic differences in physicochemical properties encountered for the same cofactor in diverse protein complexes, a critical factor for all biological functions must be the close structural interplay between bound cofactors and the respective apoprotein in addition to factors such as hydrogen bonding or electronic effects. Here, we explore how nature can use the same chemical molecule as a cofactor for chemically distinct reactions using the concept of conformational flexibility of tetrapyrroles.
    [Show full text]
  • Mode of Action Uncovered for the Specific Reduction of Methane Emissions from Ruminants by the Small Molecule 3-Nitrooxypropanol
    Correction AGRICULTURAL SCIENCES, ENVIRONMENTAL SCIENCES Correction for “Mode of action uncovered for the specific re- duction of methane emissions from ruminants by the small mol- ecule 3-nitrooxypropanol,” by Evert C. Duin, Tristan Wagner, Seigo Shima, Divya Prakash, Bryan Cronin, David R. Yáñez-Ruiz, Stephane Duval, Robert Rümbeli, René T. Stemmler, Rudolf Kurt Thauer, and Maik Kindermann (first published May 2, 2016; 10.1073/pnas.1600298113). The authors note that Fig. 1 appeared incorrectly. The cor- rected figure and its legend appear below. CORRECTION Fig. 1. Methane formation in the rumen of a dairy cow and its inhibition by 3-nitrooxypropanol (3-NOP). The H2 concentration in the rumen fluid is near 1 μM(≙ 140 Pa = 0.14% in the gas phase). www.pnas.org/cgi/doi/10.1073/pnas.1607088113 www.pnas.org PNAS | May 31, 2016 | vol. 113 | no. 22 | E3185 Downloaded by guest on September 25, 2021 Mode of action uncovered for the specific reduction of methane emissions from ruminants by the small molecule 3-nitrooxypropanol Evert C. Duina, Tristan Wagnerb, Seigo Shimab, Divya Prakasha,1, Bryan Cronina, David R. Yáñez-Ruizc, Stephane Duvald, Robert Rümbelie, René T. Stemmlere, Rudolf Kurt Thauerb,2, and Maik Kindermanne,2 aDepartment of Chemistry and Biochemistry, Auburn University, Auburn, AL 36849; bMax Planck Institute for Terrestrial Microbiology, D-35043 Marburg, Germany; cEstación Experimental del Zaidín, Consejo Superior de Investigaciones Cientificas, 18008 Granada, Spain; dResearch Centre for Animal Nutrition and Health, DSM Nutritional Products France, 68305 Saint Louis, France; and eResearch and Development, DSM Nutritional Products, 4002 Basel, Switzerland Edited by Lonnie O.
    [Show full text]