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Tetrapyrroles structure

There are hundreds of iron-containing enzymes. In general, the iron can exist as (a) a mononuclear site, in which it is coordinated by a tetrapyrrole structure (hemes) or strictly by amino acid residues that donate oxo, nitrogen, or sulfur ligands (b) a dinuclear site in which the irons are bridged by oxo, nitrogen, or sulfur coordination (c) a trinuclear site as in the 3Fe-4S clusters or (d) a tetranuclear site as in the [4Fe-4S] clusters. [Pg.284]

The tetrapyrrole structure characteristic of the porphyrins is produced in the next steps of the synthetic pathway. Hydroxyme-thylbilane synthase catalyzes the linkage of four porphobilinogen molecules and cleavage of an NH2 group to yield uroporphyrinogen III. [Pg.192]

The tetrapyrrole structure of uroporphyrinogen III is still very different from that of heme. For example, the central iron atom is missing, and the ring contains only eight of the 11 double bonds. In addition, the ring system only carries charged R side chains (four acetate and four propionate residues). As heme groups have to act in the apolar interior of proteins, most of the polar side... [Pg.192]

To quantitate and analyze conjugated bile pigments, azo derivative formation is applied most frequently (Fig. 1). Such terms as azobilirubin, or azobilirubin conjugate, erroneously suggest tetrapyrrolic structures. The following trivial names appear to be more appropriate dipyrromethene azo derivative, azodipyrrole, dipyrrolic azo pigment, and the like. The term azodipyrrole will be employed in the present review. [Pg.245]

Cytochrome P-450 from rat or human liver microsome preparations is inactivated when incubated anaerobically with carbon tetrachloride in the presence of NADPH and an oxygen-scavenging system (Manno et al. 1988 1992). Inactivation involved destruction of the heme tetrapyrrolic structure, and followed pseudo first-order kinetics with fast and slow half lives of 4.0 and 29.8 minutes. When compared with rat liver microsomes, the human preparations were 6-7 times faster at metabolizing carbon tetrachloride, and only about one- eighth as susceptible to suicide inactivation (about 1 enzyme molecule lost for every 196 carbon tetrachloride molecules metabolized). [Pg.69]

Once the porphyrin ring is open, the metal is deposited on the catalyst. Open chain tetrapyrrolic structures (M-biliverdenates) are unstable under catalytic hydrogenation conditions (Subramanian and Fuhrhop, 1978). The ease of this sequence with Ni-etioporphyrin (Ni-etio) is apparent by the lack of stable metal intermediates other than the chlorin (M-PH2). [Pg.162]

Heme degradation Bile pigments exist in both the plant and animal kingdoms, and are formed by breakdown of the cyclic tetrapyrrole structure of heme. In animals this pathway is an excretory system by which the heme from the hemoglobin of aging red blood cells, and other hemoproteins, is removed from the body. In the plant kingdom, however, heme is broken down to form bile pigments... [Pg.388]

Similar reactions occur in red algae and cyanobacteria but because the full spectrum of sunlight does not always penetrate very far below the surface of the sea they make use of different pigments. These may be structurally similar to those used by plants, and are therefore classed as bacteriochlorophylls, or belong to the structurally distinct phycobilin class of compounds. Unlike chlorophyll, which has a cyclic tetrapyrrole structure containing magnesium, the phycobilins are acyclic tetrapyrroles with similarities to the breakdown product of the haem ring, bilirubin. [Pg.137]

The general cyclic tetrapyrrole structure of a heme ring is shown below ... [Pg.404]

F-430 A tetrapyrrole structure containing nickel, a component of the ENZYME methyl-coenzyme M REDUCTASE, that is involved in the formation of methane in METHANOGENIC bacteria. The highly reduced macro-cyclic structure, related to porphyrins and corrins, is termed a corphin. [Pg.105]

Figure 31 -20 Bilirubin IXa structure. Top, The unfolded or linear tetrapyrrole structure showing the Z bonds. Bottom, The folded conformation showing extensive internal hydrogen bonding. (Reftr/nfed by permission of Elsevier Science Publishing Co., Inc., from Schmid, R. Bilirubin metabolism State of the art. Gastroenterology 1978 74 1307-12, with permission from the American Gastroenterological Association.)... Figure 31 -20 Bilirubin IXa structure. Top, The unfolded or linear tetrapyrrole structure showing the Z bonds. Bottom, The folded conformation showing extensive internal hydrogen bonding. (Reftr/nfed by permission of Elsevier Science Publishing Co., Inc., from Schmid, R. Bilirubin metabolism State of the art. Gastroenterology 1978 74 1307-12, with permission from the American Gastroenterological Association.)...
Porphyrins are heteroaromatic compounds characterised by a tetrapyrrolic structure that consists of four pentagonal pyrroles linked by four methylene bridges, the porphine structure (Figure 1). [Pg.61]

A a,c,d B a,b,c,d C a. The bilin pigments are linear tetrapyrroles, structurally related to bilirubin and biliverdin, the pigments found in bruises and largely responsible for the yellow color of jaundiced skin. See pages 688 and 689 in the text to compare these structures. It may be easier to remember the terms phycoerythrobilin and phycocyanobilin if you know that in Greek erythro means red and cyano means blue. ... [Pg.338]

The macrocyclic tetrapyrrole structure of porphyrins was first suggested in 1912 by Kiister. At the time, Hans Fischer and others thought that such a ring was too large to be stable. Not until 1929, when Fischer and his Munich School of chemists achieved their classical total synthesis of heme, was this structure finally accepted. Fischer then went on to devise many synthetic routes to porphyrins starting from pyrroles and dipjnrrolic compounds... [Pg.48]

Benzochlorin 50 consists of a benzene ring fused to the tetrapyrrolic structure and was first reported by Arnold et from octaethylporphyrin H2(OEP) in several steps such as, formylation, Wittig reaction, reduction and oxidation. Morgan et al. followed this approach and benzochlorins 54 and 55, as major and minor products, respectively, were obtained (Scheme 15). [Pg.172]

Until the mid-1970s the four classic cyclic tetrapyrrolic structures with their porphyrin, chlorin, bacteriochlorin, and corrin skeletons were almost the only representatives in the class of porphyrinoid natural products 1-10). Although other partially reduced porphyrins were conceivable, none of these partially saturated porphyrinoid structures had hitherto been found in nature. [Pg.3]

Diekert G, Jaenchen R, Thauer RK (1980) Biosynthetic evidence for a Nickel tetrapyrrole structure of Factor F430 from Methanobacterium thermoautotrophicum. FEBS Lett. 119 118... [Pg.49]

It is worth emphasizing the importance of the (III) oxidation state of copper, obtained by using a tetrapyrrolic structure, and its relationship with copper(II) mediated... [Pg.200]

A complex of iron in which the organic component is not a porphyrin, but a related tetrapyrrole structure, e. g. verdoheme, biliverdin heme. [Pg.280]

HPIX is a macrocycUc tetrapyrrole structure with four methyl, two propionic acid, and two ethanolic sidechains. The two propionic acid and two ethanolic chains react with Group IVB metallocene dichlorides, giving crosslinked polymers as 11. [Pg.83]


See other pages where Tetrapyrroles structure is mentioned: [Pg.579]    [Pg.26]    [Pg.71]    [Pg.235]    [Pg.603]    [Pg.323]    [Pg.324]    [Pg.248]    [Pg.387]    [Pg.91]    [Pg.297]    [Pg.247]    [Pg.3952]    [Pg.753]    [Pg.753]    [Pg.1193]    [Pg.158]    [Pg.60]    [Pg.1474]    [Pg.641]    [Pg.647]    [Pg.421]    [Pg.3495]    [Pg.331]   
See also in sourсe #XX -- [ Pg.485 ]




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