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| | Aberration of heme and hemoprotein in aged female rats. |
 | | The activities of hexobarbital hydroxylase and aniline hydroxylase, indicators of mono-oxygenase function, were decreased in aged rats by 31% and 24%, respectively, as compared to values in young rats. | | | The pharmacological effectiveness of many drugs is altered during the aging process. | | | The magnitude and duration of drug action is determined partially by the activity of the drug metabolizing enzyme systems in the liver. |
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http://www.arclab.org/medlineupdates/abstract_3600051.html
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| | Hemoprotein Examples |
| | Notice that they all are involved in some way with oxygen or with oxidation processes. | | | Also given is information about their turnover to emphasize the need for resynthesis of the protein and the heme. | | | These are only a few of the many hemoproteins. |
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http://www.porphyrin.net/Heme_iron/importance.html
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| | hemoprotein metabolism |
| | sum of chemical changes that occur within the tissues of an organism consisting of anabolism (biosynthesis) and catabolism of hemoproteins; the buildup and breakdown of hemoproteins for utilization by the organism. |
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http://crisp.cit.nih.gov/Thesaurus/00003686.htm
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| | Structural studies of sirohaem-Fe4S4 enzymes |
| | Janick, P.A., Rueger, D.C., Krueger, R.J., Barber, M.J. and Siegel, L.M. Characterization of complexes between Escherichia coli sulfite reductase hemoprotein subunit and its substrates sulfite and nitrite. | | | Pierik, A.J. and Hagen, W.R. =9/2 EPR signals are evidence against coupling between the siroheme and the Fe/S cluster prosthetic groups in Desulfovibrio vulgaris (Hildenborough) dissimilatory sulfite reductase. | | | Siegel, L.M., Rueger, D.C., Barber, M.J., Krueger, R.J., OrmeJohnson, N.R. and OrmeJohnson, W.H. Escherichia coli sulfite reductase hemoprotein subunit. |
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http://metallo.scripps.edu/PROMISE/SIROHAEM_REF.html
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| | Julian A. Peterson, Ph.D. |
| | To understand the details of the structure-function relationships within and between the two classes, structural studies on additional cytochromes P450 are crucial. | | | The research conducted in the Peterson Laboratory is supported in part by research grants GM43479 and GM50858 from the National Institutes of Health. | | | Cytochromes P450 are members of a superfamily of hemoproteins that are involved in the metabolism of various physiologic and xenobiotic organic compounds. |
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http://www.swmed.edu/home_pages/peterlab/ref18.htm
(265 words)
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| | OCA Atlas for 2HPD |
| | Bacillus Megaterium) Recombinant Form Expressed In (Escherichia Coli) | | | Crystal structure of hemoprotein domain of P450BM-3, a prototype for microsomal P450's., Ravichandran KG, Boddupalli SS, Hasermann CA, Peterson JA, Deisenhofer J, Science 1993 Aug 6;261(5122):731-6. | | | Nadph + n oxidized hemoprotein = nadp(+) + n reduced hemoprotein. |
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http://oca.ebi.ac.uk/oca-bin/ocashort?id=2hpd
(430 words)
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| | Hemoprotein - Wikipedia, the free encyclopedia |
| | Hemoproteins are found in such diverse roles as: | | | A hemoprotein (also haemoprotein), or heme protein, is a metalloprotein containing a heme prosthetic group, either covalently or noncovalently bound to the protein itself. | | | This page was last modified 15:53, 28 January 2006. |
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http://en.wikipedia.org/wiki/Hemoprotein
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| | (WO 00/02580) THERAPIES USING HEMOPROTEINS |
| | The NO-consuming activity of a hemoprotein (e.g., a flavorhemoglobin) can be used in a treatment where constriction of blood vessels is desirable, or where it is otherwise desirable to reduce NO concentration, as in inflammation. | | | The method can be used to treat a mammal having pathologically proliferating cells, such as a tumor. | | | The method of the invention comprises administering a therapeutically effective amount of a hemoprotein having NO-activated deoxygenase activity or an enzymatically active fragment thereof to a mammal. |
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http://wipo.int/cgi-pct/guest/getbykey5?KEY=00/02580.000120&ELEMENT_SET=DECL
(242 words)
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| | Nature |
| | The resulting FixJ-phosphate linkage is sensitive to base, like the aspartyl phosphates found in homologous systems. | | | The finding that FixL is a hemoprotein with kinase activity raises a major question as to whether or not the oxygenation state of the heme moiety affects its kinase activity. | | | Oxygen Sensor FixL, from the Two-Component FixL/FixJ system of Rhizobium meliloti, is a Novel Hemoprotein with Kinase Activity |
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http://www.biosci.ohio-state.edu/~mgonzalez/nature/nature.html
(2423 words)
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| | Myoglobin - Wikipedia, the free encyclopedia |
| | Its specificity and the cost of the analysis has prevented its widespread use. | | |   "Myoglobin: an essential hemoprotein in striated muscle" by George A. Ordway1 and Daniel J. Garry in Journal of Experimental Biology (2004) Volume 207, pages 3441-3446. |
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http://en.wikipedia.org/wiki/Myoglobin
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| | Julian A. Peterson, Ph.D. |
| | The results indicate there is a considerable alteration of P450 IIB1 when it is put into the phosphorylation medium. | | | This includes destruction, i.e., loss of the hemoprotein nature (Soret peak), as well as denaturation, conversion of a proportion of the P450 to P420. | | | Suggestions are made that this structural modification caused by cytochrome b5 stabilizes the P450 against denaturation as well as against destruction and phosphorylation. |
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http://www.swmed.edu/home_pages/peterlab/ref31.htm
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| | heme |
| | The hemoprotein family represents a fascinating example of how similar metal-based prosthetic groups can perform many different specific functions, depending on the protein environment. | | | Pavone “Peptide Based Hemoprotein Model” Chem Rev. 101, 3165-3189 (2001) | | | With the aim of investigating the effects of peptide chain composition and folding in modulating the properties of the heme, we have undertaken the design, synthesis and spectroscopic characterization of a new class of heme-peptide conjugates named |
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http://chemistry.unina.it/bioinorganic/heme.html
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| | Energy Citations Database (ECD) - Energy and Energy-Related Bibliographic Citations |
| | Availability information may be found in the Availability, Publisher, Research Organization, Resource Relation and/or Author (affiliation information) fields and/or via the "Full-text Availability" link. | | | Energy Citations Database (ECD) Document #6460452 - Green hemoprotein of erythrocytes: methemoglobin superoxide transferase |
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http://www.osti.gov/energycitations/product.biblio.jsp?osti_id=6460452
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| | EC 1.6.2.4 |
| | The number n in the equation is 1 if the hemoprotein undergoes a 2-electron reduction, and is 2 if it undergoes a 1-electron reduction. |
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http://www.chem.qmul.ac.uk/iubmb/enzyme/EC1/6/2/4.html
(344 words)
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| | [No title] |
| | HEADER OXIDOREDUCTASE(OXYGENASE) 16-SEP-93 2HPD COMPND CYTOCHROME P450 (BM-3) (E.C.1.14.14.1) (HEMOPROTEIN DOMAIN) COMPND 2 (FATTY ACID MONOOXYGENASE) SOURCE (BACILLUS MEGATERIUM) RECOMBINANT FORM EXPRESSED SOURCE 2 IN (ESCHERICHIA COLI) AUTHOR K.G.RAVICHANDRAN,S.S.BODDUPALLI,C.A.HASEMANN,J.A.PETERSON, AUTHOR 2 J.DEISENHOFER REVDAT 1 31-OCT-93 2HPD 0 JRNL AUTH K.G.RAVICHANDRAN,S.S.BODDUPALLI,C.A.HASEMANN, JRNL AUTH 2 J.A.PETERSON,J.DEISENHOFER JRNL TITL CRYSTAL STRUCTURE OF HEMOPROTEIN DOMAIN OF |
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http://www.bmm.icnet.uk/loop/hdr/2hpd.txt
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| | David R. Benson |
| | 4) Kennedy, M.L.; Silchenko, S.; Houndonougbo, N.; Gibney, B.R.; Dutton, P.L.; Rodgers, K.R.; Benson, D.R. “Model Hemoprotein Reduction Potentials: The Effects of Histidine to Iron Coordination Equilibrium” J. | | | 3) Lee, K.-H.; Kennedy, M.L.; Buchalova, M.; Benson, D.R. “Thermodynamics of Carbon Monoxide Binding by Helical Hemoprotein Models: The Effect of a Competing Intramolecular Ligand” Tetrahedron 2000, 56, 9725-9732. | | | 2) Liu, D.; Williamson, D.A.; Kennedy, M.L.; Williams, T.D.; Morton, M.M.; Benson, D.R. “Aromatic Side Chain-Porphyrin Interactions in Designed Hemoproteins” J. |
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http://www.chem.ku.edu/dbenson
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| | Sessler Group: Publications |
| | Sessler, J. L.; Collman, J. "The 'Pocket' Porphyrins: Hemoprotein Models with Lowered CO Affinities," Kagaku 1984, 39, 805-806. | | | J.; Iverson, B.; Sessler, J. "The 'Pocket' Porphyrin: A Hemoprotein Model with Lowered CO Affinity," J. Am. | | | J.; Iverson, B. I.; Sessler, J. L.; Morris, R.; Gibson, Q. "The 'Pocket' Porphyrins: Hemoprotein Models with Lowered CO Affinities," Inorg. |
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http://research.cm.utexas.edu/jsessler/publications.html
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| | [No title] |
| | ID STRID %IDE %WSIM IFIR ILAS JFIR JLAS LALI NGAP LGAP LSEQ2 ACCNUM PROTEIN 1 : CYSI_ECOLI 8GEP 1.00 1.00 99 459 209 569 361 0 0 569 P17846 Sulfite reductase [NADPH] hemoprotein bet 2 : Q8X7U2 1.00 1.00 99 459 210 570 361 0 0 570 Q8X7U2 Sulfite reductase, alpha subunit. | | | 26 : Q6D1A2 0.85 0.90 1 46 87 132 46 0 0 577 Q6D1A2 Sulfite reductase [NADPH] hemoprotein bet 27 : Q7N8L5 0.85 0.91 1 46 81 126 46 0 0 576 Q7N8L5 Sulfite reductase. | | | 120 : Q8KQT8 0.51 0.59 1 46 73 117 45 1 1 573 Q8KQT8 Sulfite reductase hemoprotein. |
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http://www.infobiogen.fr/db/hssp/6gep.hssp
(2119 words)
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