Notes on Lamission.Edu

Total Page:16

File Type:pdf, Size:1020Kb

Notes on Lamission.Edu 1 Plants are AUTOTROPHS in that they make their own food and thus sustain themselves without consuming organic molecules derived from any other organisms. Plant cells capture light energy, and convert it to chemical energy. Using this energy, plants make their own organic molecules and are the ultimate source of organic molecules for almost all other organisms. They are often referred to as the PRODUCERS of the biosphere because they produce its food supply. All organisms that produce organic molecules from inorganic molecules using the energy of light are called PHOTOAUTOTROPHS. In this chapter we focus on photosynthesis in plants, which takes place in chloroplasts. The process of photosynthesis most likely originated in a group of bacteria that had infolded regions of the plasma membrane containing such clusters of enzymes and molecules. Chloroplasts appear to have originated from a photosynthetic prokaryote that lived inside a eukaryotic cell. 2 All green parts of a plant have chloroplasts in their cells and can carry out photosynthesis. Their green color is from CHLOROPHYLL, a light absorbing pigment in the chloroplasts that plays a central role in converting solar energy to chemical energy. Chloroplasts are concentrated in the cells of the mesophyll, the green tissue in the interior of the leaf. Carbon dioxide enters the leaf and oxygen exists, by way of tiny pores called STOMATA. Water absorbed by the roots is delivered to the leaves in veins. 3 An envelope of two membranes encloses an inner compartment in the chloroplast, which is filled with a thick fluid called STROMA. Suspended in the stroma is a system of interconnected membranous sacs, called THYLAKOIDS, which enclose another compartment, called the thylakoid space. In some places, thylakoids are concentrated in stacks called GRANA. Built into the thylakoid membranes are the chlorophyll molecules that capture light. 4 In the 1800’s most scientists assumed that plants produce O2 by extracting it from CO2. In the 1950’s, scientists tested this hypothesis by using a heavy isotope of oxygen,18O, to follow the fate of oxygen atoms during photosynthesis. EXPERIMENT 1: a plant given carbon dioxide containing 18O gave off no labeled oxygen gas (18O containing). EXPERIMENT 2: a Plant given water containing 18O did produce labeled O2. These experiments showed that the O2 produced during photosynthesis comes from water and not from CO2. It takes two water (H2O) molecules to make each molecule of O2. Additional experiments have revealed that the oxygen atoms in CO2 and the hydrogens in the reactant H2O molecules end up in the sugar molecule and in water that is formed anew. 5 Photosynthesis is a redox (oxidation-reduction) process, just as cellular respiration is. In photosynthesis, water molecules are split apart, yielding O2, they are actually oxidized; that is, they loose electrons, along with hydrogen ions (H+). Meanwhile, CO2 is reduced to sugar as electrons and hydrogen ions are added to it. Overall Cellular respiration harvests energy stored in a glucose molecule by oxidizing the sugar and reducing O2 to H2O. This process involves a number of energy-releasing redox reactions, with electrons losing potential energy as they travel down an energy “hill” from sugar to O2. In contrast, the food-producing redox reactions of photosynthesis involve an uphill climb. As water is oxidized and CO2 is reduced during photosynthesis, electrons gain energy by being boosted up an energy hill. The light energy captured by chlorophyll molecules in the chloroplast provides the boost for the electrons. Photosynthesis converts light energy to chemical energy and stores it in the chemical bonds of sugar molecules, which can provide energy for later use or raw materials for biosynthesis. 6 Photosynthesis occurs in two stages, each with multiple steps. The LIGHT REACTIONS include the steps that convert light energy to chemical energy and produce O2. The light reaction occur in the thylakoid membranes. Water is split, providing a source of electrons and giving off O2 gas as a by-product. Light energy absorbed by chlorophyll molecules built into the membranes is sued to drive the transfer of electrons and H+ from water to NADP+, reducing it to NADPH. NADPH is an electron carrier similar to NADH that transports electrons in cellular respiration. In summary the light reactions of photosynthesis are the steps that absorb solar energy and convert it to chemical energy stored in ATP and NADPH. Notice that these reactions produce no sugar; sugar is not made until the CASLVIN CYCL, the second stage of photosynthesis. The CALVIN CYCLE occurs in the stroma of the chloroplast. It is a cyclic series of reactions that assemble sugar molecules using CO2 and the energy-containing products of the light reactions. In the 1940’s, Calvin and his colleagues traced the path of carbon in the cycle, using the radioactive isotope 14C to label the carbon in CO2. The incorporation of carbon from CO2 into organic compounds is called CARBON FIXATION. After carbon fixation, enzymes of the cycle make sugars by further reducing the carbon compounds. It is NADPH produced by the light reactions that provides the electrons for reducing carbon in the Calvin cycle. And ATP from the light reaction provides chemical energy that powers several of the steps of the Calvin cycle. The Calvin cycle is sometimes referred to as the dark reactions, or light-independent reactions, because none of the steps requires light directly. 7 Sunlight is a type of energy called ELECTROMAGNETIC ENERGY or RADIATION. Electromagnetic spectrum, is the full range of electromagnetic wavelengths from the very short gamma rays to the very long-wavelength radio waves. Visible light- the radiation your eyes see as different colors- is only a small fraction of the spectrum. It consists of wavelengths from about 380 nm to about 750 nm. The distance between the crests of two adjacent waves is called a WAVELENGTH. Shorter wavelength have more energy than longer ones. The theory of light as waves explains most of light’s properties. However, light also behaves as discrete packets of energy called photons. PHOTONS is a fixed quantity of light energy, and as you have just learned, the shorter the wavelength, the greater the energy. 8 Light-absorbing molecules called pigments, built into the thylakoid membranes, absorb some wavelengths of light and reflect or transmit other wavelengths. We do not see the absorbed wavelengths; their energy has been absorbed by pigment molecules. What we see when we look at a leaf are the green wavelengths that the pigment transmits and reflects. Different pigments absorb light of different wavelengths, and chloroplasts contain several kinds of pigments. Chlorophyll a, which participates directly in the light reactions, absorbs mainly blue-violet and red light. A very similar molecule chlorophyll b absorbs mainly blue and orange light and reflects yellow-green. Chloroplasts also contain a family of pigments called CAROTENOIDS, which seem to be used in photoprotection: They absorb and dissipate excessive light energy that would otherwise damage chlorophyll or interact with oxygen to form reactive oxidative molecules that can damage cell molecules. 9 When a pigment molecule absorbs a photon, one of the pigment’s electron’s jumps to an energy level farther from the nucleus. In this location, the electron has more potential energy, and we say that the electron has been raised from a ground state to an excited state. The excited state is very unstable. Chlorophyll in its native habitat of the thylakoid membrane, passes off its excited electron to a neighboring molecule before it has a chance to drop back to the ground state. In the thylakoid membrane, chlorophyll molecules are organized along with other pigments and proteins into clusters called photosystems. A photosystem consists of a number of light-harvesting complexes surrounding a reaction center complex. The light-harvesting complexes consist of pigment molecules bound to proteins. The REACTION CENTER COMPLEX contains a pair of chlorophyll a molecules and a molecule called the primary electron acceptor, which is capable of accepting electrons and becoming reduced. Two types of photosystems have been identified, and they cooperate in the light reactions. They are referred to as Photosystem 1 and photosystem 2, with photosystem 2 acting first. In photosystem 2 the chlorophyll a of the reaction center is called P680 because the light it absorbs best is red light with a wavelength of 680nm. The reaction center chlorophyll of photosystem 1 is called P700 nm. 10 In the light reactions, light energy is transformed into the chemical energy of ATP and NADPH. In this process, electrons removed from water molecules pass from photosystem 2 to photosystem 1 to NADP+. Between the two photosystems, the electrons move down an electron transport chain and provide energy for the synthesis of ATP. 1.) A pigment molecule in a light-harvesting complex absorbs a photon of light. The energy is passed to other pigment molecules and finally to the reaction center of photosystem 2, where it excites an electron of chlorophyll P680 to a higher energy state. 2.) This electron is captured by the primary electron acceptor. 3.) Water is split, and its electrons are supplied one by one to P680, each replacing an electron lost to the primary electron acceptor. The oxygen atom combines with an oxygen oxygen from another split water molecule to form a molecule of O2. 4.) Each photoexcited electron passes from photosystem 2 to photosystem 1 via an electron transport chain. The exergonic “fall” of electrons provides energy for the synthesis of ATP by pumping H+ across the membrane. 5.) Light energy excites an electron of chlorophyll P700 in the reaction center of photosystem 1. The primary electron center captures the electron, and an electron from the bottom of the electron transport chain replaces the lost electron in P700.
Recommended publications
  • Light-Induced Psba Translation in Plants Is Triggered by Photosystem II Damage Via an Assembly-Linked Autoregulatory Circuit
    Light-induced psbA translation in plants is triggered by photosystem II damage via an assembly-linked autoregulatory circuit Prakitchai Chotewutmontria and Alice Barkana,1 aInstitute of Molecular Biology, University of Oregon, Eugene, OR 97403 Edited by Krishna K. Niyogi, University of California, Berkeley, CA, and approved July 22, 2020 (received for review April 26, 2020) The D1 reaction center protein of photosystem II (PSII) is subject to mRNA to provide D1 for PSII repair remain obscure (13, 14). light-induced damage. Degradation of damaged D1 and its re- The consensus view in recent years has been that psbA transla- placement by nascent D1 are at the heart of a PSII repair cycle, tion for PSII repair is regulated at the elongation step (7, 15–17), without which photosynthesis is inhibited. In mature plant chloro- a view that arises primarily from experiments with the green alga plasts, light stimulates the recruitment of ribosomes specifically to Chlamydomonas reinhardtii (Chlamydomonas) (18). However, we psbA mRNA to provide nascent D1 for PSII repair and also triggers showed recently that regulated translation initiation makes a a global increase in translation elongation rate. The light-induced large contribution in plants (19). These experiments used ribo- signals that initiate these responses are unclear. We present action some profiling (ribo-seq) to monitor ribosome occupancy on spectrum and genetic data indicating that the light-induced re- cruitment of ribosomes to psbA mRNA is triggered by D1 photo- chloroplast open reading frames (ORFs) in maize and Arabi- damage, whereas the global stimulation of translation elongation dopsis upon shifting seedlings harboring mature chloroplasts is triggered by photosynthetic electron transport.
    [Show full text]
  • Evolution of Photochemical Reaction Centres
    bioRxiv preprint doi: https://doi.org/10.1101/502450; this version posted December 20, 2018. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY 4.0 International license. 1 Evolution of photochemical reaction 2 centres: more twists? 3 4 Tanai Cardona, A. William Rutherford 5 Department of Life Sciences, Imperial College London, London, UK 6 Correspondence to: [email protected] 7 8 Abstract 9 The earliest event recorded in the molecular evolution of photosynthesis is the structural and 10 functional specialisation of Type I (ferredoxin-reducing) and Type II (quinone-reducing) reaction 11 centres. Here we point out that the homodimeric Type I reaction centre of Heliobacteria has a Ca2+- 12 binding site with a number of striking parallels to the Mn4CaO5 cluster of cyanobacterial 13 Photosystem II. This structural parallels indicate that water oxidation chemistry originated at the 14 divergence of Type I and Type II reaction centres. We suggests that this divergence was triggered by 15 a structural rearrangement of a core transmembrane helix resulting in a shift of the redox potential 16 of the electron donor side and electron acceptor side at the same time and in the same redox direction. 17 18 Keywords 19 Photosynthesis, Photosystem, Water oxidation, Oxygenic, Anoxygenic, Reaction centre 20 21 Evolution of Photosystem II 22 There is no consensus on when and how oxygenic photosynthesis originated. Both the timing and the 23 evolutionary mechanism are disputed.
    [Show full text]
  • Chapter 3 the Title and Subtitle of This Chapter Convey a Dual Meaning
    3.1. Introduction Chapter 3 The title and subtitle of this chapter convey a dual meaning. At first reading, the subtitle Photosynthetic Reaction might seem to indicate that the topic of the structure, function and organization of Centers: photosynthetic reaction centers is So little time, so much to do exceedingly complex and that there is simply insufficient time or space in this brief article to cover the details. While this is John H. Golbeck certainly the case, the subtitle is Department of Biochemistry additionally meant to convey the idea that there is precious little time after the and absorption of a photon to accomplish the Molecular Biology task of preserving the energy in the form of The Pennsylvania State University stable charge separation. University Park, PA 16802 USA The difficulty is there exists a fundamental physical limitation in the amount of time available so that a photochemically induced excited state can be utilized before the energy is invariably wasted. Indeed, the entire design philosophy of biological reaction centers is centered on overcoming this physical, rather than chemical or biological, limitation. In this chapter, I will outline the problem of conserving the free energy of light-induced charge separation by focusing on the following topics: 3.2. Definition of the problem: the need to stabilize a charge-separated state. 3.3. The bacterial reaction center: how the cofactors and proteins cope with this problem in a model system. 3.4. Review of Marcus theory: what governs the rate of electron transfer in proteins? 3.5. Photosystem II: a variation on a theme of the bacterial reaction center.
    [Show full text]
  • Chlorophyll Biosynthesis
    Chlorophyll Biosynthesis: Various Chlorophyllides as Exogenous Substrates for Chlorophyll Synthetase Jürgen Benz and Wolfhart Rüdiger Botanisches Institut, Universität München, Menziger Str. 67, D-8000 München 19 Z. Naturforsch. 36 c, 51 -5 7 (1981); received October 10, 1980 Dedicated to Professor Dr. H. Merxmüller on the Occasion of His 60th Birthday Chlorophyllides a and b, Protochlorophyllide, Bacteriochlorophyllide a, 3-Acetyl-3-devinylchlo- rophyllide a, Pyrochlorophyllide a, Pheophorbide a The esterification of various chlorophyllides with geranylgeranyl diphosphate was investigated as catalyzed by the enzyme chlorophyll synthetase. The enzyme source was an etioplast membrane fraction from etiolated oat seedlings ( Avena sativa L.). The following chlorophyllides were prepared from the corresponding chlorophylls by the chlorophyllase reaction: chlorophyllide a (2) and b (4), bacteriochlorophyllide a (5), 3-acetyl-3-devinylchlorophyllide a (6), and pyro­ chlorophyllide a (7). The substrates were solubilized with cholate which reproducibly reduced the activity of chlorophyll synthetase by 40-50%. It was found that the following compounds were good substrates for chlorophyll synthetase: chlorophyllide a and b, 3-acetyl-3-devinylchloro- phyllide a, and pyrochlorophyllide a. Only a poor or no reaction was found with protochloro­ phyllide, pheophorbide a, and bacteriochlorophyllide. This difference of reactivity was not due to distribution differences of the substrates between solution and pelletable membrane fraction. Furthermore, no interference between good and poor substrate was detected. Structural features necessary for chlorophyll synthetase substrates were discussed. Introduction Therefore no exogenous 2 was applied. The only substrate was 2 formed by photoconversion of endo­ The last steps of chlorophyll a (Chi a) biosynthe­ genous Protochlide (1) in the etioplast membrane.
    [Show full text]
  • Bilirubin: an Animal Pigment in the Zingiberales and Diverse Angiosperm Orders Cary L
    Florida International University FIU Digital Commons FIU Electronic Theses and Dissertations University Graduate School 11-5-2010 Bilirubin: an Animal Pigment in the Zingiberales and Diverse Angiosperm Orders Cary L. Pirone Florida International University, [email protected] DOI: 10.25148/etd.FI10122201 Follow this and additional works at: https://digitalcommons.fiu.edu/etd Part of the Biochemistry Commons, and the Botany Commons Recommended Citation Pirone, Cary L., "Bilirubin: an Animal Pigment in the Zingiberales and Diverse Angiosperm Orders" (2010). FIU Electronic Theses and Dissertations. 336. https://digitalcommons.fiu.edu/etd/336 This work is brought to you for free and open access by the University Graduate School at FIU Digital Commons. It has been accepted for inclusion in FIU Electronic Theses and Dissertations by an authorized administrator of FIU Digital Commons. For more information, please contact [email protected]. FLORIDA INTERNATIONAL UNIVERSITY Miami, Florida BILIRUBIN: AN ANIMAL PIGMENT IN THE ZINGIBERALES AND DIVERSE ANGIOSPERM ORDERS A dissertation submitted in partial fulfillment of the requirements for the degree of DOCTOR OF PHILOSOPHY in BIOLOGY by Cary Lunsford Pirone 2010 To: Dean Kenneth G. Furton College of Arts and Sciences This dissertation, written by Cary Lunsford Pirone, and entitled Bilirubin: An Animal Pigment in the Zingiberales and Diverse Angiosperm Orders, having been approved in respect to style and intellectual content, is referred to you for judgment. We have read this dissertation and recommend that it be approved. ______________________________________ Bradley C. Bennett ______________________________________ Timothy M. Collins ______________________________________ Maureen A. Donnelly ______________________________________ John. T. Landrum ______________________________________ J. Martin Quirke ______________________________________ David W. Lee, Major Professor Date of Defense: November 5, 2010 The dissertation of Cary Lunsford Pirone is approved.
    [Show full text]
  • Coexistence of Phycoerythrin and a Chlorophyll A/B Antenna in a Marine Prokaryote (Prochlorophyta/Cyanobacteria/Phycobilins/Photosynthesis/Endosymbiosis) WOLFGANG R
    Proc. Natl. Acad. Sci. USA Vol. 93, pp. 11126-11130, October 1996 Microbiology Coexistence of phycoerythrin and a chlorophyll a/b antenna in a marine prokaryote (Prochlorophyta/cyanobacteria/phycobilins/photosynthesis/endosymbiosis) WOLFGANG R. HESs*t, FREDEIRIC PARTENSKYt, GEORG W. M. VAN DER STAAYI, JOSE' M. GARCIA-FERNANDEZt, THOMAS BORNER*, AND DANIEL VAULOTt *Department of Biology, Humboldt-University, Chausseestrasse 117, D-10115 Berlin, Germany; and tStation Biologique de Roscoff, Centre National de la Recherche Scientifique Unite Propre de Recherche 9042 and Universite Pierre et Marie Curie, BP 74, F-29682 Roscoff Cedex, France Communicated by Hewson Swift, The University of Chicago, Chicago, IL, July 1Z 1996 (received for review June 7, 1996) ABSTRACT Prochlorococcus marinus CCMP 1375, a ubiq- tation maximum of the major chromophore bound by PE-III uitous and ecologically important marine prochlorophyte, corresponds to that of phycourobilin. was found to possess functional genes coding for the a and 1 subunits of a phycobiliprotein. The latter is similar to phy- coerythrins (PE) from marine Synechococcus cyanobacteria MATERIALS AND METHODS and bind a phycourobilin-like pigment as the major chro- Flow Cytometric Measurements. Sea water samples were mophore. However, differences in the sequences of the ca and collected at different depths during the France-Joint Global 13 chains compared with known PE subunits and the presence Ocean Flux Study OLIPAC cruise held in November 1994 of a single bilin attachment site on the a subunit designate it aboard the N.O. l'Atalante. Samples were analyzed immedi- as a novel PE type, which we propose naming PE-III. P. ately using a FACScan (Becton Dickinson) flow cytometer and marinus is the sole prokaryotic organism known so far that cell concentrations of Prochlorococcus and Synechococcus contains chlorophylls a and b as well as phycobilins.
    [Show full text]
  • Quantify Chlorophyll a and Chlorophyll B with a Custom Method
    APPLICATION NOTE NanoDrop One/OneC No. T141 Quantify chlorophyll a and chlorophyll b with a custom method Using the NanoDrop One Spectrophotometer Abstract Scientists can accurately quantify chlorophyll a and chlorophyll b on the Thermo Scientific™ NanoDrop™ One/OneC Microvolume UV-Vis Spectrophotometer using a user-defined custom method. Introduction Chlorophyll a is the principal pigment that converts light energy to chemical energy, and chlorophyll b is the accessory photosynthetic pigment that transfers light it absorbs to chlorophyll a. Chlorophyll a is found in all plants, green algae, and cyanobacteria, and chlorophyll b is found in plants and green algae. Chlorophyll quantitation is valuable in a vast array of disciplines including but not limited to plant biology, environmental science, ecotoxicology, disease prevention, and medical drug discovery. Spectrophotometry is a common method used to measure the absorbance of light by the chlorophyll molecules. The NanoDrop One/OneC UV-Vis Spectrophotometer can be used to measure the absorbance of chlorophyll. Chlorophyll a and chlorophyll b absorb light at slightly different wavelengths. peaks (Figure 1). With this information, a user-defined Chlorophyll a absorbs light at 433 nm and 666 nm custom method including user-defined formulas can be and chlorophyll b absorbs light at 462 nm and 650 created to measure the absorbance and determine the nm. The NanoDrop One/OneC UV-Vis application can concentration of chlorophyll. be used to observe the spectrum of each chlorophyll a and chlorophyll b and identify major absorbance chlorophyll a Figure 2. Chlorophyll Content custom method created to quantify chlorophyll a and chlorophyll b samples suspended in 100% DMSO.
    [Show full text]
  • Standard Operating Procedure for Chlorophyll a Sampling Method Field Procedure
    Standard Operating Procedure for Chlorophyll a Sampling Method Field Procedure LG404 Revision 07, March 2013 TABLE OF CONTENTS Section Number Subject Page 1.0.............SCOPE AND APPLICATION..................................................................................................1 2.0.............SUMMARY OF METHOD ......................................................................................................1 3.0.............APPARATUS .............................................................................................................................1 4.0.............REAGENTS................................................................................................................................1 5.0.............SAMPLE HANDLING AND PRESERVATION ...................................................................1 6.0.............FIELD PROCEDURE ...............................................................................................................2 7.0.............QUALITY ASSURANCE .........................................................................................................2 8.0.............SAFETY AND WASTE HANDLING ......................................................................................3 9.0.............SHIPPING ..................................................................................................................................3 Disclaimer: Mention of trade names or commercial products does not constitute endorsement or recommendation for use. Standard Operating
    [Show full text]
  • Effects of Iron and Oxygen on Chlorophyll Biosynthesis' I
    Plant Physiol. (1982) 69, 107-1 1 1 0032-0889/82/69/0107/05/$00.50/0 Effects of Iron and Oxygen on Chlorophyll Biosynthesis' I. IN VIVO OBSERVATIONS ON IRON AND OXYGEN-DEFICIENT PLANTS Received for publication March 31, 1981 and in revised form July 31, 1981 SUSAN C. SPILLER, ANN M. CASTELFRANCO2, AND PAUL A. CASTELFRANCOQ Department ofBotany, University of Cal!fornia, Davis, California 95616 ABSTRACT ALA4 (3). It is probable that this in vivo 02 requirement, in part, reflects the need for molecular O2 in aerobic respiration, which is Corn (Zea mnays, L.), bean (Phaseolus vulgaris L.), barley (Hordeum necessary to generate ATP in the common test plants (e.g. cucum- vudgare L.), spinach (Spuiacia oeracea L.), and sugarbeet (Beta vulgaris ber, bean, barley). L.) grown under iron deficiency, and Potamogeton pectinatus L, and Pota- In the present paper we are reporting on: (a) the accumulation mogeton nodosus Poir. grown under oxygen deficiency, contained less of Mg-Proto(Me) in vivo by Fe and 02-deficient plants; (b) the chlorophyll than the controls, but accumulated Mg-protoporphyrin IX and/ effect of Fe and O2 deficiency on the conversion of exogenous or Mg-protoporphyrin IX monomethyl ester. No significant accumulation ALA to Pchlide by plant tissue segments. The following article by of these intermediates was detected in the controls or in the tissue of Chereskin and Castelfranco (5) deals with the inhibition of ALA plants stressed by S, Mg, N deficiency, or by prolonged dark treatment. synthesis by Fe- and Mg-containing tetrapyrroles, and the effects Treatment of normal plant tissue with 8-aminolevulinic acid in the dark of Fe-chelators and anaerobiosis on the conversion of Mg-Proto resulted in the accumulation of protochlorophyliide.
    [Show full text]
  • Catabolism of Tetrapyrroles As the Final Product of Heme Catabolism (Cf Scheme 1)
    CHEMIE IN FREIBURG/CHIMIE A FRIBOURG 352 CHIMIA 48 (199~) Nr. 9 (Scl'lcmhcr) ns itu Chimia 48 (/994) 352-36/ heme (1), at the a-methene bridge (C(5)) €> Neue Sclnveizerische Chemische Gesellschaft producing CO and an unstable Felli com- /SSN 0009-4293 plex. The latter loses the metal ion to yield the green pigment protobiliverdin IXa (usually abbreviated to biliverdin (2)), which is excreted by birds and amphibia, Catabolism of Tetrapyrroles as the final product of heme catabolism (cf Scheme 1). The iron is recovered in the protein called ferritin and can be reutilized Albert Gossauer* for the biosynthesis of new heme mole- cules. As biliverdin (2) has been recog- nized to be a precursor in the biosynthesis of phycobilins [9], a similar pathway is Abstract. The enzymatic degradation of naturally occurring tetrapyrrolic pigments probably followed for the biosynthesis of (heme, chlorophylls, and vitamin B 12) is shortly reviewed. this class oflight-harvesting chromophores 1. Introduction pounds known so far are synthesized, have Scheme I. Catabolism (!{ Heme ill Mammals been already elucidated, it may be antici- In contrast to the enormous amount of pated that the study of catabolic processes work accomplished by chemists in the will attract the interest of more chemists elucidation of biosynthetic pathways of and biochemists in the near future. secondary metabolites (terpenes, steroids, alkaloids, among others), only a few at- tempts have been made until now to un- 2. Heme Catabolism derstand the mechanisms oftheirdegrada- tion in living organisms. A possible rea- It has been known for over half a cen- son for this fact is the irrational association tury that heme, the oxygen-carrier mole- of degradation (catabolism: greek Kara= cule associated with the blood pigment down) with decay and, thus, with unattrac- hemoglobin, is converted in animal cells tive dirty colors and unpleasant odors.
    [Show full text]
  • A Stromal Region of Cytochrome B6f Subunit IV Is Involved in the Activation of the Stt7 Kinase in Chlamydomonas
    A stromal region of cytochrome b6f subunit IV is involved in the activation of the Stt7 kinase in Chlamydomonas Louis Dumasa, Francesca Zitob, Stéphanie Blangya, Pascaline Auroya, Xenie Johnsona, Gilles Peltiera, and Jean Alrica,1 aLaboratoire de Bioénergétique et Biotechnologie des Bactéries et Microalgues, Commissariat à l’Energie Atomique et aux Energies Alternatives (CEA), CNRS, Aix-Marseille Université, UMR 7265, Institut de Biosciences et Biotechnologies d’Aix-Marseille, CEA Cadarache, F-13108 Saint-Paul-lez-Durance, France; and bLaboratoire de Biologie Physico-Chimique des Protéines Membranaires, Institut de Biologie Physico-Chimique, CNRS, UMR7099, University Paris Diderot, Sorbonne Paris Cité, Paris Sciences et Lettres Research University, F-75005 Paris, France Edited by Jean-David Rochaix, University of Geneva, Geneva 4, Switzerland, and accepted by Editorial Board Member Joseph R. Ecker September 25, 2017 (received for review July 28, 2017) The cytochrome (cyt) b6f complex and Stt7 kinase regulate the and PQH2 binding are required (10, 17, 18), the PetO subunit of antenna sizes of photosystems I and II through state transitions, cyt b6f is phosphorylated by Stt7 during PQ pool reduction (19), which are mediated by a reversible phosphorylation of light har- and the lumenal domain of Stt7 interacts directly with the vesting complexes II, depending on the redox state of the plasto- Rieske-ISP subunit of cyt b6f and contains two conserved cyste- quinone pool. When the pool is reduced, the cyt b6f activates the ine residues (20). However, the Stt7 kinase domain (20) and Stt7 kinase through a mechanism that is still poorly understood. After Stt7-dependent LHCII phosphorylation sites (21) are located on random mutagenesis of the chloroplast petD gene, coding for subunit the stromal side of the membrane.
    [Show full text]
  • 1801.Full.Pdf
    Proc. Natl. Acad. Sci. USA Vol. 75, No. 4, pp. 1801-1804, April 1978 Botany Photosynthetic characteristics and organization of chlorophyll in marine dinoflagellates (photosynthesis/chlorophyll-proteins/photosynthetic unit/algae/light-harvesting) BARBARA B. PREZELIN* AND RANDALL S. ALBERTEO * Department of Biological Sciences and Marine Science Institute, University of California, Santa Barbara, California 93106; and t Department of Biology, Barnes Laboratory, The University of Chicago, Chicago, Illinois 60637 Communicated by Paul J. Kramer, February 2,1978 ABSTRACT- The photosystem I reaction center complex, unrelated to pigmentation (3) and undergo photosynthetic the P-700-chlorophyll a-protein, has been isolated from the photoadaptive responses characterized by increased pigmen- photosynthetic membranes of two marine dinoflagellates, tation and a Gonyaulax polyedra and Glenodinium sp., by detergent solu- maintenance of photosynthetic capacity at lower bilization with Triton X-100. The complexes isolated from the light levels (1, 2). two species were indistinguishable, exhibiting identical ab- In the present study we asked specifically how is chlorophyll sorption properties (400-700 nm) at both room (300 K) and low functionally organized in the photosynthetic unit in these algae (77 K) temperature. The room temperature, red wavelength and is this organization related to the ability of these dino- maximum was at 675 nm. The absorption properties, kinetics flagellates to light-adapt, to and to out of photobleaching, sodium dodecyl sulfate
    [Show full text]