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Biochemistry 37 — Mechanism-based inactivation of P 2A6 by furanocoumarins. Laemmli, U. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature — Lee, B. Isolation of an outer membrane he-min-binding protein of Haemophilus influenzae type b.

Lindenmayer, A.

Hemoprotein

Low temperature spectral studies on the biosynthesis of cytochromes in bakers yeast. List, B. Klatt, E. Werner, K. Schmidt, and B. Overexpression of neuronal nitric oxide synthase in insect cells reveals requirement of haem for tetrahydrobiopterin binding. Maines, M. The heme oxygenase system: a regulator of second messenger gases. Mayer, B. Klatt, B.

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List, C. Harteneck, and K. Large-scale purification of rat brain nitric oxide synthase from baculovirus overexpression system. McMillan, K. Bredt, D. Hirsch, S. Snyder, J. Clark, and B. Cloned, expressed rat cerebellar nitric oxide synthase contains stoichiometric amounts of heme, which binds carbon monoxide. USA 89 — Salerno, and B. Nitric oxide synthases: analogies to cytochrome P monooxygenases and characterization of recombinant rat neuronal nitric oxide synthase hemoprotein.

Miller, J. Photoafnnity labeling of cytochrome P 2B4: capture of active site heme ligands by a photocarbene. Miyake, Y. Spectral intermediates during the reduction of hepatic microsomal cytochrome P Tokyo 79 — Modi, S. Paine, M. Sutdiffe, L. Lian, W. Primrose, C. Wolf, and G. A model for human cytochrome P 2D6 based on homology modeling and NMR studies of substrate binding. Biochemistry 35 — Mok, T. Rickard, and F.

The carbon monoxide-reactive haemoproteins of yeast. Muchmore, D. McIntosh, C. Russell, D. Anderson, and F. Expression and nitrogen labeling of proteins for proton and nitrogen nuclear magnetic resonance. Nagai, K. Generation of betaglo-bin by sequence-specific proteolysis of a hybrid protein produced in Escherichia coli. Nakane, M. Pollock, V. Klinghofer, F. Basha, R. Marsden, A. Hokari, T. Ogura, H. Esumi, and G. Functional expression of three isoforms of human nitric oxide synthase in baculovirus-infected insect cells.

North, J. Dietrich, and A. Multicomponent analysis of heme protein spectra in biological materials. Ohnishi, T. Miura, and Y. Photoaffinity labeling of cytochrome P beta with methyltrienolone as a probe for the substrate binding region. Ortiz de Montellano, P. Arylhydrazines as probes of hemoprotein structure and function. Bio-chimie 77 — Nishida, I. Rodriguez-Crespo, and N. Nitric oxide synthase structure and electron transfer.

Structure and mechanism of heme oxygenase. Osawa, Y. Nakatsuka, M. Williams, J. Kindt, and M. Reactions of reactive metabolites with hemoproteins-toxicological implications: covalent alteration of hemoproteins. Otto, B. Nuijens, J. Luirink, and B. Characterization of a hemoglobin protease secreted by the pathogenic Escherichia coli strain EB1. Pollock, W. Rosell, M. Twitchett, M. Dumont, and A. Bacterialexpression of a mitochondrial cytochrome c.

Trimethylation of lys72 in yeast isocytochrome c and the alkaline con-formational transition. Poole, R. Scott, and B. Low-temperature spectral and kinetic properties of cytochromes in Escherichia coli K grown at lowered oxygen tension. Poulos, T.


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Modeling of mammalian Ps on basis of Pcam X-ray structure. Ramos, L. Beebe, W. Karey, M. Sanches, B. Erickson, B. Wilson, B. Wangen, and B. Renaud, J. Davydov, K. Heirwegh, D. Mansuy, and G. Hui Bon Hoa. Thermodynamic studies of substrate binding and spin transitions in human cytochrome P 3A4 expressed in yeast microsomes. Rieske, J. The quantitative determination of mitochondrial hemoproteins. Ristau, O. Rein, S. Greschner, G. Janig, and K. Quantitative analysis of the spin equilibrium of cytochrome P LM2 fraction from rabbit liver microsomes.

Acta Biol. Rivera, M. Barillas-Mury, K. Christensen, J. Little, M. Wells, and F. Gene synthesis, bacterial expression, and 1H NMR spectroscopic studies of the rat outer mitochondrial membrane cytochrome b5. Riveros-Moreno, V. Heffernan, B. Torres, A. Chubb, I. Charles, and S. Purification to homogeneity and characterisation of rat brain recombinant nitric oxide synthase. Rodgers, K. Heme-based sensors in biological systems [In Process Citation].

Rodriguez-Crespo, I. Gerber, and P. Endothelial nitric-oxide synthase. Expression in Escherichia coli , spectroscopic characterization, and role of tetrahydrobiopterin in dimer formation. Roman, L. Sheta, P. Martasek, S. Gross, Q. Liu, and B. High-level expression of functional rat neuronal nitric oxide synthase in Escherichia coli.

USA 92 — Sari, M. Booker, M. Jaouen, S. Vadon, J. Boucher, D. Pompon, and D. Expression in yeast and purification of functional macrophage nitric oxide synthase. Evidence for cysteine as iron proximal ligand. Sarma, S. DiGate, D. Banville, and R. NMR 8 — Schmidt, M. Enzymatic detection of native and derivatized horseradish peroxidase in sodium dodecyl sulfate polyacrylamide gels. Schuller, D. Wilks, P. Ortiz de Montellano, and T. Crystal structure of human heme oxygenase Seo, H.

Fujii, H. Soejima, N. Niikawa, and N. Heme requirement for production of active endothelial nitric oxide synthase in baculovirus-infected insect cells. Shelver, D. Thorsteinsson, R. Kerby, S. Chung, G. Roberts, M. Reynolds, R. Parks, and J. Identification of two important heme site residues cysteine 75 and histidine 77 in CooA, the CO-sensing transcription factor of Rhodospirillum rubrum.

Shen, T. Ho, V. Simplaceanu, M. Zou, B. Green, M. Tam, and C. Production of unmodified human adult hemoglobin in Escherichia coli. USA 90 — Shioi, Y. Takamiya, and M. Studies on energy and electron transfer systems in green photosynthetic bacterium Chloropseudomonas ethylica strain 2K. Isolation and characterization of cytochromes from Chloropseudomonas ethylica strain 2K.

Tokyo 71 — Shrager, R. Shu, F. Ramakrishnan, and B. High-level expression and deuteration of sperm whale myoglobin. A study of its solvent structure by X-ray and neutron diffraction methods. Basic Life Sci. Smith, A. Santama, S. Dacey, M. Edwards, R. Bray, R. Thorneley, and J. Smulevich, G. Mauro, L. Fishel, A. English, J. Kraut, and T. Heme pocket interactions in cytochrome c peroxidase studied by site-directed mutagenesis and resonance Raman spectroscopy.

Biochemistry 27 — Conformational change and histidine control of heme chemistry in cytochrome c peroxidase: resonance Raman evidence from Leu and Gly mutants of cytochrome c peroxidase. Biochemistry 30 — Spiro, T. Resonance Raman spectra of hemoproteins. Resonance Raman spectroscopy as a probe of heme protein structure and dynamics. Resonance Raman spectroscopy of metalloproteins. Springer, B. High-level expression of sperm whale myoglobin in Escherichia coli. USA 84 — Sun, J. Resonance Raman and EPR spectroscopic studies on heme-heme oxygenase complexes.

Biochemistry 32 — Tamburini, P. Gibson, W. Backes, S. Sligar, and J. Reduction kinetics of purified rat liver cytochrome P Evidence for a sequential reaction mechanism dependent on the hemoprotein spin state. Biochemistry 23 — Taylor, K. Uhlinger, and J. Kinkade, Jr. Expression of recombinant myeloperoxidase using a baculovirus expression system. Teale, F. Cleavage of the haem-protein link by acid methyl ethyl ketone. Teraoka, J. Structural implication of the heme-linked ionization of horseradish peroxidase probed by the Fe-histidine stretching Raman line.

Thomas, P. Ryan, and W. An improved staining procedure for the detection of the peroxidase activity of cytochrome P on sodium dodecyl sulfate polyacrylamide gels. Tschirret-Guth, R. Medzihradszky, and P. Specific azidophenyl-diazene hemoprotein active site probes. Cross-linking of the heme to His in myoglobin. Trifluoromethyl-diazirinylphenyldiazenes: new hemeprotein active-site probes. Ortiz de Motellano.

Background

Synthesis of photoaffinity probes for heme-containing proteins. Tsutsui, K.

Heme and Hemoproteins - Semantic Scholar

Affinity chromatography of heme-binding proteins: synthesis of hemin-agarose. A protein with multiple heme-binding sites from rabbit serum. Varadarajan, R. Szabo, and S. Cloning, expression in Escherichia coll , and reconstitution of human myoglobin. USA 52 — Vickery, L. Spin states of heme proteins by magnetic circular dichroism. Richardson, J. Cosme, and E. Microsomal P 2C3 is expressed as a soluble dimer in Escherichia coli following modification of its N-terminus. Vuletich, J. Chemiluminescence assay for oxidatively modified myoglobin. Wilks, A. Black, W. Miller, and P.

Expression and characterization of truncated human heme oxygenase hHO-1 and a fusion protein of hHO-1 with human cytochrome P reductase. Biochemistry 34 — Intramolecular translocation of the protein radical formed in the reaction of recombinant sperm whale myoglobin with H 2 O 2.

Rat liver heme oxygenase. High level expression of a truncated soluble form and nature of the meso-hydroxy-lating species. Expression and characterization of a heme oxygenase Hmu O from Corynebacterium diphtheriae. Iron acquisition requires oxidative cleavage of the heme macrocycle.

Torpey, and P. Heme oxygenase HO Evidence for electrophilic oxygen addition to the porphyrin ring in the formation of alpha-meso-hydroxyheme. Wu, C. Zhang, H. Abu-Soud, D. Ghosh, and D. High-level expression of mouse inducible nitric oxide synthase in Escherichia coli requires coexpression with calmodulin.

Yoshida, T. Ishikawa, and M. Degradation of heme by a soluble peptide of heme oxygenase obtained from rat liver microsomes by mild trypsinization. Purification and properties of heme oxygenase from pig spleen microsomes. Yun, C. Hammons, G. Sato, and T. Expression of rat heme oxygenase in Escherichia coli as a catalytically active, full-length form that binds to bacterial membranes. Jennings, P. Stone, and P. Overexpression of myoglobin and assignment of its amide, C alpha and C beta resonances. Jones, S. Tasab, J. Ogden, D. Ballance, and M. Expression of rat neuronal nitric oxide synthase in Saccharomyces cerevisiae.


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Jung, C. Ristau, and H. Kakuno, T. Bartsch, K. Nishikawa, and T. Redox componenets associated with chromatophores from Rhodospirillum rubrum. Kincaid, J. Stein, and T. Absence of heme-localized strain in T state hemoglobin: insensitivity of heme-imidazole resonance Raman frequencies to quaternary structure. USA 76 — King, M. The respiratory electron transport system of heterotrophically-grown Rhodopseudomonas palustris. Kitagawa, T. Nagai, and M. Assignment of the Fe-Nepsilon His F8 stretching band in the resonance Raman spectra of deoxy myoglobin. FEBS Lett. Knaff, D. Cytochrome b and photosynthetic sulfur bacteria.

Koenigs, L. Mechanism-based inactivation of cytochrome P 2B1 by 8-methoxypsoralen and several other furanocoumarins. Biochemistry 37 — Mechanism-based inactivation of P 2A6 by furanocoumarins. Laemmli, U. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature — Lee, B. Isolation of an outer membrane he-min-binding protein of Haemophilus influenzae type b. Lindenmayer, A. Low temperature spectral studies on the biosynthesis of cytochromes in bakers yeast. List, B. Klatt, E. Werner, K. Schmidt, and B. Overexpression of neuronal nitric oxide synthase in insect cells reveals requirement of haem for tetrahydrobiopterin binding.

Maines, M. The heme oxygenase system: a regulator of second messenger gases. Mayer, B. Klatt, B. List, C. Harteneck, and K. Large-scale purification of rat brain nitric oxide synthase from baculovirus overexpression system. McMillan, K. Bredt, D. Hirsch, S. Snyder, J. Clark, and B. Cloned, expressed rat cerebellar nitric oxide synthase contains stoichiometric amounts of heme, which binds carbon monoxide.

USA 89 — Salerno, and B. Nitric oxide synthases: analogies to cytochrome P monooxygenases and characterization of recombinant rat neuronal nitric oxide synthase hemoprotein. Miller, J. Photoafnnity labeling of cytochrome P 2B4: capture of active site heme ligands by a photocarbene. Miyake, Y. Spectral intermediates during the reduction of hepatic microsomal cytochrome P Tokyo 79 — Modi, S.

Paine, M. Sutdiffe, L. Lian, W. Primrose, C. Wolf, and G. A model for human cytochrome P 2D6 based on homology modeling and NMR studies of substrate binding. Biochemistry 35 — Mok, T. Rickard, and F. The carbon monoxide-reactive haemoproteins of yeast. Muchmore, D. McIntosh, C. Russell, D. Anderson, and F.

Expression and nitrogen labeling of proteins for proton and nitrogen nuclear magnetic resonance. Nagai, K. Generation of betaglo-bin by sequence-specific proteolysis of a hybrid protein produced in Escherichia coli. Nakane, M. Pollock, V. Klinghofer, F. Basha, R. Marsden, A. Hokari, T. Ogura, H. Esumi, and G. Functional expression of three isoforms of human nitric oxide synthase in baculovirus-infected insect cells. North, J. Dietrich, and A. Multicomponent analysis of heme protein spectra in biological materials. Ohnishi, T. Miura, and Y.

Photoaffinity labeling of cytochrome P beta with methyltrienolone as a probe for the substrate binding region. Ortiz de Montellano, P. Arylhydrazines as probes of hemoprotein structure and function. Bio-chimie 77 — Nishida, I. Rodriguez-Crespo, and N. Nitric oxide synthase structure and electron transfer. Structure and mechanism of heme oxygenase. Osawa, Y. Nakatsuka, M. Williams, J. Kindt, and M. Reactions of reactive metabolites with hemoproteins-toxicological implications: covalent alteration of hemoproteins. Otto, B. Nuijens, J. Luirink, and B.

Characterization of a hemoglobin protease secreted by the pathogenic Escherichia coli strain EB1. Pollock, W.

The Heme Group and Hemoglobin Part 2

Rosell, M. Twitchett, M. Dumont, and A. Bacterialexpression of a mitochondrial cytochrome c. Trimethylation of lys72 in yeast isocytochrome c and the alkaline con-formational transition. Poole, R. Scott, and B. Low-temperature spectral and kinetic properties of cytochromes in Escherichia coli K grown at lowered oxygen tension. Poulos, T. Modeling of mammalian Ps on basis of Pcam X-ray structure.

Ramos, L. Beebe, W. Karey, M. Sanches, B. Erickson, B. Wilson, B. Wangen, and B. Renaud, J. Davydov, K. Heirwegh, D. Mansuy, and G. Hui Bon Hoa. Thermodynamic studies of substrate binding and spin transitions in human cytochrome P 3A4 expressed in yeast microsomes. Rieske, J. The quantitative determination of mitochondrial hemoproteins. Ristau, O. Rein, S. Greschner, G. Janig, and K. Quantitative analysis of the spin equilibrium of cytochrome P LM2 fraction from rabbit liver microsomes.

Acta Biol. Rivera, M. Barillas-Mury, K. Christensen, J. Little, M. Wells, and F. Gene synthesis, bacterial expression, and 1H NMR spectroscopic studies of the rat outer mitochondrial membrane cytochrome b5. Riveros-Moreno, V. Heffernan, B. Torres, A. Chubb, I. Charles, and S. Purification to homogeneity and characterisation of rat brain recombinant nitric oxide synthase. Rodgers, K. Heme-based sensors in biological systems [In Process Citation]. Rodriguez-Crespo, I. Gerber, and P. Endothelial nitric-oxide synthase.

Expression in Escherichia coli , spectroscopic characterization, and role of tetrahydrobiopterin in dimer formation. Roman, L. Sheta, P. Martasek, S. Gross, Q. Liu, and B. High-level expression of functional rat neuronal nitric oxide synthase in Escherichia coli. USA 92 — Sari, M. Booker, M. Jaouen, S. Vadon, J. Boucher, D.

Pompon, and D. Expression in yeast and purification of functional macrophage nitric oxide synthase. Evidence for cysteine as iron proximal ligand. Sarma, S. DiGate, D. Banville, and R. NMR 8 — Schmidt, M. Enzymatic detection of native and derivatized horseradish peroxidase in sodium dodecyl sulfate polyacrylamide gels. Schuller, D. Wilks, P. Ortiz de Montellano, and T. Crystal structure of human heme oxygenase Seo, H. Fujii, H. Soejima, N. Niikawa, and N. Heme requirement for production of active endothelial nitric oxide synthase in baculovirus-infected insect cells.

Shelver, D. Thorsteinsson, R. Kerby, S. Chung, G. Roberts, M. Reynolds, R. Parks, and J. Identification of two important heme site residues cysteine 75 and histidine 77 in CooA, the CO-sensing transcription factor of Rhodospirillum rubrum. Shen, T. Ho, V. Simplaceanu, M. Zou, B. Green, M. Tam, and C. Production of unmodified human adult hemoglobin in Escherichia coli. USA 90 — Shioi, Y. Takamiya, and M. Studies on energy and electron transfer systems in green photosynthetic bacterium Chloropseudomonas ethylica strain 2K.

Isolation and characterization of cytochromes from Chloropseudomonas ethylica strain 2K. Tokyo 71 — Shrager, R. Shu, F. Ramakrishnan, and B. High-level expression and deuteration of sperm whale myoglobin. A study of its solvent structure by X-ray and neutron diffraction methods. Basic Life Sci. Smith, A. Santama, S. Dacey, M. Edwards, R. Bray, R. Thorneley, and J. Smulevich, G. Mauro, L.

Fishel, A. English, J. Kraut, and T. Heme pocket interactions in cytochrome c peroxidase studied by site-directed mutagenesis and resonance Raman spectroscopy. Biochemistry 27 — Conformational change and histidine control of heme chemistry in cytochrome c peroxidase: resonance Raman evidence from Leu and Gly mutants of cytochrome c peroxidase. Biochemistry 30 — Spiro, T.

Resonance Raman spectra of hemoproteins. Resonance Raman spectroscopy as a probe of heme protein structure and dynamics. Resonance Raman spectroscopy of metalloproteins. Springer, B. High-level expression of sperm whale myoglobin in Escherichia coli. USA 84 — Sun, J. Resonance Raman and EPR spectroscopic studies on heme-heme oxygenase complexes. Biochemistry 32 — Tamburini, P. Gibson, W. Backes, S. Sligar, and J. Reduction kinetics of purified rat liver cytochrome P Evidence for a sequential reaction mechanism dependent on the hemoprotein spin state. Biochemistry 23 — Taylor, K.

Uhlinger, and J. Kinkade, Jr. Expression of recombinant myeloperoxidase using a baculovirus expression system. Teale, F. Cleavage of the haem-protein link by acid methyl ethyl ketone. Teraoka, J. Structural implication of the heme-linked ionization of horseradish peroxidase probed by the Fe-histidine stretching Raman line. Thomas, P. Ryan, and W. An improved staining procedure for the detection of the peroxidase activity of cytochrome P on sodium dodecyl sulfate polyacrylamide gels.

Tschirret-Guth, R. Medzihradszky, and P. Specific azidophenyl-diazene hemoprotein active site probes. Cross-linking of the heme to His in myoglobin. Trifluoromethyl-diazirinylphenyldiazenes: new hemeprotein active-site probes. Ortiz de Motellano. Synthesis of photoaffinity probes for heme-containing proteins. Tsutsui, K. Affinity chromatography of heme-binding proteins: synthesis of hemin-agarose.

A protein with multiple heme-binding sites from rabbit serum. Varadarajan, R. Szabo, and S. Cloning, expression in Escherichia coll , and reconstitution of human myoglobin. USA 52 — Vickery, L.