Cytochrome c oxidase, the terminal enzyme of the respiratory chains of mitochondria and aerobic bacteria, catalyzes electron transfer from cytochrome c to molecular oxygen, reducing the latter to water. Electron transfer is coupled to proton translocation across the membrane, resulting in a proton and charge gradient that is then employed by the. Structure of cytochrome oxidase (1OCC) in the inner mitochondrial membrane. Cytochrome oxidase is a transmembrane protein in the inner mitochondrial membrane. It is a dimer with two identical chemical units containing two hemes, three coppers, magnesium and a zinc. 2 The protein is shown in ribbon depiction, with atoms of the metal-containing electron transport centers shown in spheres The enzyme cytochrome c oxidase or Complex IV, EC 1.9.3.1, is a large transmembrane protein complex found in bacteria, archaea, and the mitochondria of eukaryotes. It is the last enzyme in the respiratory electron transport chain of cells located in the membrane. It receives an electron from each of four cytochrome c molecules, and transfers them to one dioxygen molecule, converting the molecular oxygen to two molecules of water. In this process it binds four protons from the.
Human cytochrome c oxidase is composed of 13 subunits. The three major subunits form the catalytic core and are encoded by mitochondrial DNA (mtDNA). The remaining subunits are nuclear-encoded. The primary sequence is known for all human subunits and the crystal structure of bovine heart cytochrome c oxidase has recently been reported Abstract. Cytochrome oxidase or cytochrome c:oxygen oxidoreductase (EC 1.9.3.1) is the terminal member of the electron-transport chain and an integral part of the mitochondrial inner membrane.It catalyzes the reaction 4H + + 4e − + O 2 ⇌ 2H 2 O; energy is released in this reaction. Under coupled conditions this energy is not dissipated as heat but is conserved and used by the ATP.
structure of the bacterial cytochrome c oxidase in a view perpendicular to the membrane normal. In this view, the cytochrome c oxidase looks like a trapezoid, with an extension at the smaller side. The trapezoid is integrated into the membrane. The extension represents the water soluble globular domain o Structure of the intact 14-subunit human cytochrome c oxidase. Respiration is one of the most basic features of living organisms, and the electron transport chain complexes are probably the most complicated protein system in mitochondria Cytochrome c oxidase--structure, function, and physiology of a redox-driven molecular machine. Richter OM(1), Cytochome c oxidase is the terminal member of the electron transport chains of mitochondria and many bacteria. Providing an efficient mechanism for dioxygen reduction on the one hand, it also acts as a redox-linked proton pump,. The most common respiratory oxidase is cytochrome c oxidase which, along with the OEC, are the subjects of intense scrutiny as attempts are made to uncover structure/function relationships. A significant roadblock to this work, the lack of detailed structural information, has recently been removed by reports of the crystal structures of a prokaryotic and a eukaryotic (mammalian) cytochrome c oxidase
Cytochrome bd (OPM family 805) is a tri-heme oxidase as it is compound by cytochromes b 558, b 595 and d. Its main function is the reduction of O 2 to H 2 O. It is thought that it uses a di-heme active site, which is formed by the hemes of cytochromes b 595 and d The thionitrobenzoate cytochrome c derivative has been shown to bind to bovine heart cytochrome-c oxidase and link covalently into subunit Mtm at C y s n 5 (Malatesta and Capaldi, 1982). This derivative also binds to CYTOCHROME-C OXIDASE STRUCTURE 105 yeast cytochrome-c oxidase, where it also links to subunit Mtm (Moreland and Docktor, 1981) Cytochrome c oxidase is a membrane protein. In the picture, notice the region between the green lines. Most of the surface atoms there are carbon (white) and sulfur (yellow). In the cell, these atoms are buried inside a membrane In cytochrome c oxidases, the subunit contains a Cu center (Cu A) with 2 Cu atoms, which is thought to be the immediate electron acceptor from cytochrome c. A possible electron transfer pathway from this center to heme a has been identified in the structure (see below). In quinol oxidases, this subunit processes the quinol substrate The most common respiratory oxidase is cytochrome c oxidase which, along with the OEC, are the subjects of intense scrutiny as attempts are made to uncover structure/function relationships. A significant roadblock to this work, the lack of detailed structural information, has recently been removed by reports of the crystal structures of a prokaryotic and a eukaryotic (mammalian) cytochrome c.
Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)) cytochrome c as the electron donor, cytochrome bo3 ubiquinol oxidase uses a membrane-soluble ubiquinol-8 (consisting of eight isoprenoid units in the hydrophobic tail) as the electron donor. Furthermore, cytochrome c oxidase contains an additional metal center, Cu A , in subunit II, whic
Structure of cytochrome oxidase from Paracoccus denitrificans. The following pictures are from Iwata et al. (1995) Cytochrome Oxidase from Paracoccus denitrificans. Nature 376 660-669; a more complete set can be found on the cytochrome oxidase home page. Click on thumbnails for larger image. Left: Cytochrome oxidase viewed from the side THE JOURNAL OF BIOI.OGICAL CHEMISTRY Vol. 253, No, 12, Issue of June 25, pp. 4389-4395, 1978 Printed in U.S.A. Structure and Orientation of Cytochrome c Oxidase i This article is cited by 48 publications. Laurence S. Romsted Jianbing Zhang, and, Lanzhen Zhuang. Mechanism of Reaction of an Arenediazonium Ion in Aqueous Solutions of Acetamide, N-Methylacetamide, and N,N-Dimethylacetamide Cytochrome r:OZ oxidoreductase (EC 1.9.3.1). ular by the heterogeneous character of the cytochrome oxidase preparations. Prerequisites for analysis of the basic quaternary structure are : (a) separation of unnecessary components, and (b) isolation of a monodisperse polypeptide complex, which makes hydrodynamic determinations possible. This wor cytochrome c oxidase. Further analysis using sequence alignments and tertiary structure analysis tools demonstrated that the hypothetical B. pseudomallei cytochrome c oxidase is similar to cytochrome c oxidases from other organisms such as Thermus thermophilus (36% protein sequence identity), Paracoccus denitrificans and bovine hear
Cytochrome oxidase : structure, function, and physiopathology / edited by Maurizio Brunori and Britton Chance Brunori, Maurizio (medarbetare) Chance, Britton (medarbetare) Università degli studi di Roma La Sapienza (medarbetare) ISBN -89766-484-1 (inb) New York, N.Y. : New York Academy of Sciences, 198 Key words: cytochrome oxidase, isoforms, yeast, oxygen,c respiration, structure, function, gene expression. Summary Introduction STRUCTURE/FUNCTION OF OXYGEN-REGULATED ISOFORMS IN CYTOCHROME c OXIDASE PATRICIA V. BURKE AND ROBERT O. POYTON* Department of Molecular, Cellular, and Developmental Biology, University of Colorado, Boulder, CO 80309. X-ray crystallographic analyses of mitochondrial cytochrome c oxidase (CcO) have been based on its dimeric form. Recent cryo-electron microscopy structures revealed that CcO exists in its monomeric form in the respiratory supercomplex. This study, using amphipol-stabilized CcO, shows that the activity of monomer is higher than that of the dimer This cytochrome oxidase is made by the bacterium Thermus thermophilus. In it, the I and III subunits are fused into one long chain, and surprisingly, cytochrome c is fused to the II subunit. In most cases, cytochrome c is a separate, soluble protein that delivers electrons to cytochrome oxidase
Structure of Cytochrome c Oxidase Fusao Takusagawa The inner mitochondrial membrane contains various proteins including redox proteins involved in electron transport and oxidative phosphorylation. In the electron-transport process, the free energy of electron transfer from NADH and FADH 2 to O 2, via protein-boun Abstract. The crystal structure of bovine heart cytochrome c oxidase at 2.8 Å resolution with an R value of 19.9 percent reveals 13 subunits, each different from the other, five phosphatidyl.. Cytochrome c oxidase is the principal terminal oxidase of high oxygen affinity in the aerobic metabolism of all animals, plants, yeasts, and some bacteria.1 It is present in the mitochondria of the more highly developed cells and in the cytoplasmic membrane of bacteria. Cytochrome c oxidase catalyzes the electron transfer from cytochrome c to O 2 Abstract. The iron-carbon monoxide stretching mode and the iron-carbon-oxygen bending mode in carbon monoxide-bound cytochrome oxidase have been assigned at 520 and 578 cm-1, respectively. The.. The eponymous cytochromes, two of type b and one of type d, are the key iron-containing groups that enable the function of oxidase. At the cytochrome d, the oxygen is bound and converted to water
While there are numerous structures of cytochrome c oxidases from a variety of species (2, 8 ⇓ ⇓ ⇓ -12), there is only 1 structure reported for a heme-copper quinol oxidase, E. coli cytochrome bo 3 ubiquinol oxidase Cytochrome c oxidase. It has been suggested that Structure, function and biosynthesis of COX be merged into this article or section. (Discuss) The enzyme cytochrome c oxidase or Complex IV (PDB 2OCC, EC 1.9.3.1) is a large transmembrane protein complex found in bacteria and the mitochondrion. Additional recommended knowledge Structure. The MT-CO2 gene is located on the p arm of mitochondrial DNA at position 12 and it spans 683 base pairs. The MT-CO2 gene produces a 25.6 kDa protein composed of 227 amino acids. MT-CO2 is a subunit of the enzyme Cytochrome c oxidase (EC 1.9.3.1) (Complex IV), an oligomeric enzymatic complex of the mitochondrial respiratory chain involved in the transfer of electrons from cytochrome. The crystal structure at 2.8 Å resolution of the four protein subunits containing cytochrome c oxidase from the soil bacterium Paracoccus denitrificans, complexed with an antibody Fvfragment, is described
Mitochondrial cytochrome c oxidase is an exceedingly complex multistructural and multifunctional membranous enzyme. In this review, we will provide an overview of the many interactions of cytochrome oxidase, stressing developments not covered by the excellent monograph of Wikström, Krab, and Saraste (1981), and continuing into early 1983 Abstract. Cytochrome‐ c oxidase was isolated from tuna liver and heart, and the subunit composition was analysed by SDS/PAGE by two separation systems. Two additional subunits of the enzyme complex were immunoprecipitated from solubilized mitochondria with an antibody against bovine subunit IV
Cytochrome c oxidase is responsible for reduction of molecular oxygen to water using reducing equivalents donated by cytochrome c and for site 3 energy coupling in oxidative phosphorylation. A mechanism-based model of the cytochrome c oxidase reaction is presented in which transfer of reducing equivalents from the lower- to the higher-potential region of the coupling site occurs against an. Learn about Cytochrome oxidase in electron transport chai It is noted that no tRNA or mirror tRNA gene was found in the 5′ upstream region of cytochrome oxidase III (COXIII) and the processing mechanism for COXIII is unknown. In the human mitochondria, the 5′ end of tRNA is cleaved by RNase P (3-5) and 3′ end of tRNA is processed by ELAC2, the mt tRNase Z (6)
Oxygen Activation and Energy Conservation by Cytochrome c Oxidase Mårten Wikström, *,† Klaas Krab,‡ and Vivek Sharma†,§ †Institute of Biotechnology, University of Helsinki, P.O. Box 56, Helsinki FI-00014, Finland ‡Department of Molecular Cell Physiology, Vrije Universiteit, P.O. Box 7161, Amsterdam1007 MC, The Netherlands §Department of Physics, University of Helsinki, P.O. Box. accelerating toward a better understanding of the structure and reactions of cytochrome c oxidase, in which heme A has a critical role (2, 3). Earlier we reported methods for the isolation and purification of heme A from bovine heart in improved yield (4) The structure-based sequence alignment of subunit I (Figure 2) between other cytochrome c oxidase sequences, the P. denitrificans and bovine heart oxidases shows that functionally vital residues, such as heme and Cu ligands or the residues proposed for the electron transfer from Cu A to the hemes, are conserved Cytochrome C oxidase deficiency (COX deficiency) is a condition that can affect several parts of the body including the skeletal muscles, heart, brain and liver. There are four types of COX deficiency differentiated by symptoms and age of onset: benign infantile mitochondrial type, French-Canadian type, infantile mitochondrial myopathy type, and Leigh syndrome Active site structure and redox processes of cytochrome c oxidase immobilised in a novel biomimetic lipid membrane on an electrode Marcel G. Friedrich , a Frank Gieβ , a Renate Naumann , a Wolfgang Knoll , a Kenichi Ataka , b Joachim Heberle , b Jana Hrabakova , c Daniel H. Murgida c and Peter Hildebrandt *
Cytochrome c oxidase (COX) is the terminal enzyme of the electron transport chain and catalyzes the transfer of electrons from cytochrome c to oxygen. COX consists of 14 subunits, three and eleven encoded, respectively, by the mitochondrial and nuclear DNA. Tissue- and condition-specific isoforms have only been reported for COX but not for the other oxidative phosphorylation complexes. The intrinsically sluggish kinetics of the oxygen reduction reaction (ORR) and overuse of expensive and unstable Pt-based catalysts have severely hampered the development of clean energy technologies. Herein, a type of non-noble metal nanozyme as an ORR electrocatalyst, with Fe-Cu dual atomic sites embedded Journal of Materials Chemistry A HOT Paper The gram-positive, thermophilic, acetogenic bacterium Moorella thermoacetica can reduce CO2 to acetate via the Wood-Ljungdahl (acetyl coenzyme A synthesis) pathway. This report demonstrates that, despite its classification as a strict anaerobe, M. thermoacetica contains a membrane-bound cytochrome bd oxidase that can catalyze reduction of low levels of dioxygen
INTRODUCTION. Cytochrome oxidase (Cox; EC 1.9.3.1.) is the terminal enzyme of the respiratory chain in mitochondria of eukaryotes and in many aerobic bacteria and archaea (1, 2).Located in the inner mitochondrial membrane and in the cytoplasmic membrane of prokaryotes, it receives electrons from reduced cytochrome c and transfers them to molecular oxygen as the final electron acceptor In a patient with cytochrome c oxidase deficiency (MC4DN3; 619046), Antonicka et al. (2003) identified compound heterozygosity for 2 mutations in the COX10 gene: a 791C-A transversion in exon 4, resulting in a thr196-to-lys (T196K) substitution in the second transmembrane domain of the protein, and an 878C-T transition in exon 5, resulting in a pro225-to-leu substitution (P225L; 602125.0003) 1.^ The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8 A. Tsukihara T, Aoyama H, Yamashita E, Tomizaki T, Yamaguchi H, Shinzawa-Itoh K, Nakashima R, Yaono R, Yoshikawa S. Science 272, 1136-44, (1996). View article PMID: 863815 Please note, due to the complexity of the structure this page may take longer to load . Cytochrome c oxidase is a membrane-bound enzyme that catalyses the four-electron reduction of O 2 to water, using cytochrome c as the electron donor. The active site for O 2 reduction consists of a myoglobin-like Fe-porphyrin (haem-a3) that is adjacent to a 'semi-haemocyanin-like' Cu (known as CuB.
Quaternary Structure of Bovine Cytochrome Oxidase Functional significance of cytochrome c oxidase structure The long-awaited structure of the integral membrane respiratory complex cytochrome c oxidase will now allow more precisely targeted studies designed to understand the mechanism of redox-linked proton pumping. Structure 15 October 1995, 3:981-98 Structure. The heme groups of cytochrome are similar to those of hemoglobin. Cytochrome C is a freely moving protein that shuttles electrons to complex IV, known as cytochrome oxidase
516030 - COMPLEX IV, CYTOCHROME c OXIDASE SUBUNIT I; MTCO1 - CYTOCHROME c OXIDASE I; CO1; COX1 - MT-CO1 M. J., Babcock, G. T., Gennis, R. B. Insight into the active-site structure and function of cytochrome oxidase by analysis of site-directed mutants of bacterial cytochrome aa3 and cytochrome bo. J. Bioenerg Cytochrome c oxidase (COX) is a multimeric enzyme that is located in the inner mitochondrial membrane of eukaryotes, belongs to the terminal enzymatic complex (IV) of the respiratory chain and facilitates the transfer of electrons from cytochrome c to molecular oxygen [].The three mitochondrially-encoded subunits of COX (COX1, COX2, COX3) typically possess conserved primary and secondary. Structure of cytochrome a3-Cua3 couple in cytochrome c oxidase as revealed by nitric oxide binding studies (electron paramagnetic resonance/antiferromagnetic coupling/heme proteins/copper proteins/ferroheme-NO) TOM H. STEVENS, GARY W. BRUDVIG, DAVID F. BOCIAN,.
Cytochrome oxidase: An alternative (02 reduction/metalloprotein structure/Fe(IV) heme/peroxidases) C. H. A. SEITER AND S. G. ANGELOS Department of Chemistry, University of Southern California, University Park, Los i Communicated by Martin D. Kamen, December 17, 197 Mitochondrial cytochrome c oxidase (CcO) transfers electrons from cytochrome c (Cyt.c) to O 2 to generate H 2 O, a process coupled to proton pumping. To elucidate the mechanism of electron transfer, we determined the structure of the mammalian Cyt.c-CcO complex at 2.0‐Å resolution and identified an electron transfer pathway from Cyt.c to CcO This web site. PDBj; Yorodumi; PDB-5z62; Cross-search The first figure shows the dimeric structure of (bovine) cytochrome c oxidase. This one takes a little while to load. This is a very large, membrane-bound protein. The vertical α-helices normally lie in the mitochondrial membrane (outer side of the membrane at the top) Clean and tight with light cover wear. Email to friends Share on Facebook - opens in a new window or tab Share on Twitter - opens in a new window or tab Share on Pinterest - opens in a new window or ta
cytochrome oxidase preparations from animal tissues. Table i gives the results obtained with several plant tissues. Peroxidase was tested with benzidine and hydrogen peroxide and polyphenol oxidase with catechol. Cytochrome oxidase and succinic dehydrogenase were tested spectroscopically. All plants tested were found to contain peroxidase cytochrome oxidase: n. An oxidizing enzyme that contains iron and a porphyrin and is found in the mitochondrial membrane, where it catalyzes the transfer of electrons to oxygen as part of the electron transport chain, ultimately leading to the formation of ATP Thus, the level of cytochrome c oxidase activity that is produced at different oxygen tensions in yeast is determined in part by the number of holoenzyme molecules that are assembled and in part by the oxygen-regulated isoforms of subunit V. The possibility that this type of control exists in other organisms is considered Open the structure of cytochrome c oxidase in pymol. Manipulate the structure so that it is in 'cartoon' view. a) How many different alpha helices and beta strands are in the largest subunit
At present, X-ray absoption spectroscopy is being used to determine the distances between Fe and Cu atoms of the redox center of cytochrome oxidase under conditions that ensure sample integrity even under rigorous irradiation conditions and most recently to identify the pulsed or oxygenated oxidase as having a reaction center that retains a 3.84 ± 0.05 Å Fe-Cu distance but it lacks a. Chime Messages Output 7.1.1.9 cytochrome-c oxidase IUBMB Comments An oligomeric membrane heme-Cu:O2 reductase-type enzyme that terminates the respiratory chains of aerobic and facultative aerobic organisms Cytochrome c oxidase (COX), the terminal enzyme of the mitochondrial respiratory chain, is one of the key functional and regulatory sites of the mammalian energy metabolism. Owing to the importance of the enzyme, pathogenetic mutations affecting COX frequently result in severe, often fatal metabolic disorders. No satisfactory therapy is currentl CYTOCHROME C OXIDASE: Structure and Spectroscopy CYTOCHROME C OXIDASE: Structure and Spectroscopy Michel, H.; Behr, J.; Harrenga, A.; Kannt, A. 1998-06-01 00:00:00 Cytochrome c oxidases (E.C. 1.9.3.1) are the terminal enzymes in the respiratory chains from mitochondria and many bacteria. They use the electrons of cytochrome c to reduce molecular oxygen (dioxygen)
The cytochrome oxidase activity was assayed as a measure of oxygen consumption rates using an OxyGraph oxygen electrode (Hansatech, Norfolk, UK) using either ubiquinol‐1 or N,N,N′,N′‐tetramethyl‐p‐phenylenediamine dihydrochloride (TMPD) as electron donor according to the methods described previously (Mason et al. 2009; Chen et al. 2014; Le Laz et al. 2014; Xie et al. 2014) SWISS-MODEL Repository entry for Q03736 (COX2_RHOSH), Cytochrome c oxidase subunit 2. Rhodobacter sphaeroides (Rhodopseudomonas sphaeroides Structure viewers. Molecule: EM map: Font size: [English] 日本語 menu. Structure of the intact 14-subunit human cytochrome c oxidase. Shuai Zong Ministry of Education Key Laboratory of Protein Science, Tsinghua-Peking Joint Center for Life Sciences, Beijing Advanced Innovation Center for Structural Biology, School of Life Sciences, Tsinghua University, Beijing, 100084, China
There are proton transfer pathways in the enzyme, which allow and control the access of protons, required for water formation, to the active site. One of these pathways is also used for protons to be pumped. More recently we have determined the structure of a cbb3 type cytochrome c oxidase cytochrome: [ si´to-krōm ] any of a class of hemoproteins , widely distributed in animal and plant tissue, whose main function is electron transport; distinguished. Kadenbach B: Structure and evolution of the Atmungsferment cytochrome c oxidase. Angew Chem Int Ed Engl. 1983, 22: 275-282. 10.1002/anie.198302751. Article Google Scholar 20. Napiwotzki J, Kadenbach B: Extramitochondrial ATP/ADP ratios regulate cytochrome c oxidase activity via binding to the cytosolic domain of subunit IV
The current study aied to identify cytochrome c oxidase subunit 1 (ONCOX1) in Tilapia (Oreochromis niloticus) immunized by formalin-killed Flavobacterium columnarae . Suppressive subtractive hybridization (SSH) was utilized to construct a cDNA library and a semi-quantitative RT-PCR analysis used to examine Oreochromis niloticus cytochrome c oxidase subunit 1 (COX1) gene expression The addition of NO to oxidized cytochrome c oxidase (ferrocytochrome c:oxygen oxidoreductase, EC 1.9.3.1) causes the appearance of a high-spin heme electron paramagnetic resonance (EPR) signal due to cytochrome a3. This suggests that NO coordinates to Cu{a3}+2 and breaks the antiferromagnetic couple by forming a cytochrome a3+3-Cu{a3}+2-NO complex The iron-carbon monoxide stretching mode and the iron-carbon-oxygen bending mode in carbon monoxide-bound cytochrome oxidase have been assigned at 520 and 578 cm-1, respectively.The frequencies, widths, and intensities of these modes show that the Fe-C-O grouping in carbon monoxide-cytochrome a 3 is linear but tilted from the normal to the heme plane; that the iron-histidine bond in both five.
Cytochrome C oxidase is an essential enzyme that is active in subcellular structures that help to regulate energy production (mitochondria). Four distinct forms of Cytochrome C Oxidase deficiency have been identified. The range and severity of symptoms varies greatly from case to case Close mobile search navigation. Article navigation. Volume 201, Issue A cytochrome of the a type, containing copper, that catalyzes the oxidation of 4ferrocytochrome c by molecular oxygen to 4ferricytochrome c and 2H2O. A part of Complex IV of the respiratory chain. A defic
The identity and function of these membrane-bound cytochromes have remained unknown. In this study, we demonstrate thatE. faecalis contains a cytochrome bd-type oxidase which is expressed under some growth conditions. Cytochrome bd terminal oxidase complexes are widely distributed in prokaryotes (13, 17) Destroys tertiary structure. C. Attaches to copper. D. All the above. Answer. Correct option is . A. Combines with iron. Cyanide inhibits cytochrome oxidase by combining with Iron within the enzyme which results in the prevention of transport of electrons from cytochrome oxidase to oxygen Cytochrome c oxidase deficiency is a genetic condition that can affect several parts of the body, including the muscles used for movement (skeletal muscles), the heart, the brain, or the liver.Signs and symptoms of cytochrome c oxidase deficiency usually begin before age 2 but can appear later in mildly affected individuals.. The severity of cytochrome c oxidase deficiency varies widely among. Tsukihara, T et al. 2003. The low-spin heme of cytochrome c oxidase as the driving element of the proton-pumping process. PNAS 100:15304-15309. Wilstrom M. and V. Sharma. 2018. Proton-pumping by cytochrome c oxidase- A 40-year anniversary. Elsevier 1859: 692-698. Yoshikawa, S. et al. 2012. Structural studies on bovine heart cytochrome c oxidase The crystal structure of bovine heart cytochrome c oxidase at 2.8 overset{circ}{mathrm A} resolution with an R value of 19.9 percent reveals 13 subunits, each different from the other, five phosphatidyl ethanolamines, three phosphatidyl glycerols and two cholates, two hemes A, and three copper, one magnesium, and one zinc. Of 3606 amino acid residues in the dimer, 3560 have been converged to a.
